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1. Radar Sensor Data Fitting for Accurate Linear Sprint Modelling

Author

Daniel Geneau, Patrick Cormier, Ming-Chang Tsai, Dana Agar-Newman, Seth Lenetsky, and Marc Klimstra

Subjects
velocity modelling, biomechanics, overground running, force velocity, power, Chemical technology, TP1-1185
Abstract

Background: Accurate linear sprint modelling is essential for evaluating athletes’ performance, particularly in terms of force, power, and velocity capabilities. Radar sensors have emerged as a critical tool in capturing precise velocity data, which is fundamental for generating reliable force-velocity (FV) profiles. This study focuses on the fitting of radar sensor data to various sprint modelling techniques to enhance the accuracy of these profiles. Forty-seven university-level athletes (M = 23, F = 24; 1.75 ± 0.1 m; 79.55 ± 12.64 kg) participated in two 40 m sprint trials, with radar sensors collecting detailed velocity measurements. This study evaluated five different modelling approaches, including three established methods, a third-degree polynomial, and a sigmoid function, assessing their goodness-of-fit through the root mean square error (RMSE) and coefficient of determination (r2). Additionally, FV metrics (Pmax, F0, V0, FVslope, and DRF) were calculated and compared using ANOVA. Results: Significant differences (p < 0.001) were identified across the models in terms of goodness-of-fit and most FV metrics, with the sigmoid and polynomial functions demonstrating superior fit to the radar-collected velocity data. Conclusions: The results suggest that radar sensors, combined with appropriate modelling techniques, can significantly improve the accuracy of sprint performance analysis, offering valuable insights for both researchers and coaches. Care should be taken when comparing results across studies employing different modelling approaches, as variations in model fitting can impact the derived metrics.

Published
2024
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2. A Simple and Valid Method to Calculate Wheelchair Frame Rotation Using One Wheel-Mounted IMU

Author

Marc Klimstra, Melissa Lacroix, Matt Jensen, Joel Greenshields, Daniel Geneau, Patrick Cormier, Ryan Brodie, Drew Commandeur, and Ming-Chang Tsai

Subjects
wheelchair, IMU, sport, Chemical technology, TP1-1185
Abstract

Wheelchair sports have been using Inertial Measurement Units (IMU) to measure mobility metrics during training, testing and competition. Presently, the most suitable solution to calculate wheelchair speed and frame rotation is the 3IMU method as there is uncertainty about the ability of a one wheel-mounted IMU (1IMU) approach to calculate wheelchair frame rotational kinematics. A new method for calculating wheelchair frame rotational kinematics using a single wheel-mounted IMU is presented and compared to a criterion measurement using a wheelchair-frame-mounted IMU. Goodness-of-fit statistics demonstrate very strong linear relationships between wheelchair frame angular velocity calculated from the wheel-mounted IMUs and a wheelchair-frame-mounted IMU. Root mean square error (RMSE), mean absolute error (MAE) and Bland–Altman analysis show very small differences between the wheelchair frame angular velocity calculated from the wheel-mounted IMUs and the wheelchair-frame-mounted IMU. This study has demonstrated a simple and accurate approach to estimating wheelchair frame rotation using one wheel-mounted IMU during an elite wheelchair athlete agility task. Future research is needed to reexamine and compare wheelchair mobility metrics determined using the 3IMU and 1IMU solutions using this new approach.

Published
2023
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3. Wheelchair Rugby Sprint Force-Velocity Modeling Using Inertial Measurement Units and Sport Specific Parameters: A Proof of Concept

Author

Marc Klimstra, Daniel Geneau, Melissa Lacroix, Matt Jensen, Joel Greenshields, Patrick Cormier, Ryan Brodie, Drew Commandeur, and Ming-Chang Tsai

Subjects
wheelchair, IMU, sport, Chemical technology, TP1-1185
Abstract

Background: Para-sports such as wheelchair rugby have seen increased use of inertial measurement units (IMU) to measure wheelchair mobility. The accessibility and accuracy of IMUs have enabled the quantification of many wheelchair metrics and the ability to further advance analyses such as force-velocity (FV) profiling. However, the FV modeling approach has not been refined to include wheelchair specific parameters. Purpose: The purpose of this study was to compare wheelchair rugby sprint FV profiles, developed from a wheel-mounted IMU, using current mono-exponential modeling techniques against a dynamic resistive force model with wheelchair specific resistance coefficients. Methods: Eighteen athletes from a national wheelchair rugby program performed 2 × 45 m all-out sprints on an indoor hardwood court surface. Results: Velocity modelling displayed high agreeability, with an average RMSE of 0.235 ± 0.07 m/s−1 and r2 of 0.946 ± 0.02. Further, the wheelchair specific resistive force model resulted in greater force and power outcomes, better aligning with previously collected measures. Conclusions: The present study highlights the proof of concept that a wheel-mounted IMU combined with wheelchair-specific FV modelling provided estimates of force and power that better account for the resistive forces encountered by wheelchair rugby athletes.

Published
2023
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4. eIF4B mRNA Translation Contributes to Cleavage Dynamics in Early Sea Urchin Embryos

Author

Florian Pontheaux, Sandrine Boulben, Héloïse Chassé, Agnès Boutet, Fernando Roch, Julia Morales, and Patrick Cormier

Subjects
eukaryotic initiation factor 4B, eIF4B, cell cycle, cleavage dynamics, sea urchin, early embryonic development, Biology (General), QH301-705.5
Abstract

During the first steps of sea urchin development, fertilization elicits a marked increase in protein synthesis essential for subsequent cell divisions. While the translation of mitotic cyclin mRNAs is crucial, we hypothesized that additional mRNAs must be translated to finely regulate the onset into mitosis. One of the maternal mRNAs recruited onto active polysomes at this stage codes for the initiation factor eIF4B. Here, we show that the sea urchin eIF4B orthologs present the four specific domains essential for eIF4B function and that Paracentrotus lividus eIF4B copurifies with eIF4E in a heterologous system. In addition, we investigated the role of eIF4B mRNA de novo translation during the two first embryonic divisions of two species, P. lividus and Sphaerechinus granularis. Our results show that injection of a morpholino directed against eIF4B mRNA results in a downregulation of translational activity and delays cell division in these two echinoids. Conversely, injection of an mRNA encoding for P. lividus eIF4B stimulates translation and significantly accelerates cleavage rates. Taken together, our findings suggest that eIF4B mRNA de novo translation participates in a conserved regulatory loop that contributes to orchestrating protein synthesis and modulates cell division rhythm during early sea urchin development.

Published
2022
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5. Analysis of the P. lividus sea urchin genome highlights contrasting trends of genomic and regulatory evolution in deuterostomes

Author

Ferdinand Marlétaz, Arnaud Couloux, Julie Poulain, Karine Labadie, Corinne Da Silva, Sophie Mangenot, Benjamin Noel, Albert J. Poustka, Philippe Dru, Cinta Pegueroles, Marco Borra, Elijah K. Lowe, Guy Lhomond, Lydia Besnardeau, Stéphanie Le Gras, Tao Ye, Daria Gavriouchkina, Roberta Russo, Caterina Costa, Francesca Zito, Letizia Anello, Aldo Nicosia, Maria Antonietta Ragusa, Marta Pascual, M. Dolores Molina, Aline Chessel, Marta Di Carlo, Xavier Turon, Richard R. Copley, Jean-Yves Exposito, Pedro Martinez, Vincenzo Cavalieri, Smadar Ben Tabou de Leon, Jenifer Croce, Paola Oliveri, Valeria Matranga, Maria Di Bernardo, Julia Morales, Patrick Cormier, Anne-Marie Geneviève, Jean Marc Aury, Valérie Barbe, Patrick Wincker, Maria Ina Arnone, Christian Gache, Thierry Lepage, Genoscope - Centre national de séquençage [Evry] (GENOSCOPE), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Laboratoire de Biologie du Développement de Villefranche sur mer (LBDV), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut de la Mer de Villefranche (IMEV), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), LBDV_EVOINSIDE (EvoInside), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut de la Mer de Villefranche (IMEV), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de Biologie Valrose (IBV), Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305 (LBTI), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Station biologique de Roscoff (SBR), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Biologie intégrative des organismes marins (BIOM), and Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Observatoire océanologique de Banyuls (OOB)

Subjects
[SDV.GEN.GA]Life Sciences [q-bio]/Genetics/Animal genetics, Eriçons de mar, Genòmica, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Genetics, Epigenetics, Genomics, Gene expression, Epigenètica, Biochemistry, Genetics and Molecular Biology (miscellaneous), Expressió gènica, Sea urchins, Article
Abstract

International audience; Sea urchins are emblematic models in developmental biology and display several characteristics that set them apart from other deuterostomes. To uncover the genomic cues that may underlie these specificities, we generated a chromosome-scale genome assembly for the sea urchin Paracentrotus lividus and an extensive gene expression and epigenetic profiles of its embryonic development. We found that, unlike vertebrates, sea urchins retained ancestral chromosomal linkages but underwent very fast intrachromosomal gene order mixing. We identified a burst of gene duplication in the echinoid lineage and showed that some of these expanded genes have been recruited in novel structures (water vascular system, Aristotle’s lantern, and skeletogenic micromere lineage). Finally, we identified gene-regulatory modules conserved between sea urchins and chordates. Our results suggest that gene-regulatory networks controlling development can be conserved despite extensive gene order rearrangement.

Published
2023
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6. A Peak of H3T3 Phosphorylation Occurs in Synchrony with Mitosis in Sea Urchin Early Embryos

Author

Omid Feizbakhsh, Florian Pontheaux, Virginie Glippa, Julia Morales, Sandrine Ruchaud, Patrick Cormier, and Fernando Roch

Subjects
histone phosphorylation, Haspin, mitosis, cell division, CDK1, CHR-6494, Cytology, QH573-671
Abstract

The sea urchin embryo provides a valuable system to analyse the molecular mechanisms orchestrating cell cycle progression and mitosis in a developmental context. However, although it is known that the regulation of histone activity by post-translational modification plays an important role during cell division, the dynamics and the impact of these modifications have not been characterised in detail in a developing embryo. Using different immuno-detection techniques, we show that the levels of Histone 3 phosphorylation at Threonine 3 oscillate in synchrony with mitosis in Sphaerechinus granularis early embryos. We present, in addition, the results of a pharmacological study aimed at analysing the role of this key histone post-translational modification during sea urchin early development.

Published
2020
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7. Cyclin B Translation Depends on mTOR Activity after Fertilization in Sea Urchin Embryos.

Author

Héloïse Chassé, Odile Mulner-Lorillon, Sandrine Boulben, Virginie Glippa, Julia Morales, and Patrick Cormier

Subjects
Medicine, Science
Abstract

The cyclin B/CDK1 complex is a key regulator of mitotic entry. Using PP242, a specific ATP-competitive inhibitor of mTOR kinase, we provide evidence that the mTOR signalling pathway controls cyclin B mRNA translation following fertilization in Sphaerechinus granularis and Paracentrotus lividus. We show that PP242 inhibits the degradation of the cap-dependent translation repressor 4E-BP (eukaryotic initiation factor 4E-Binding Protein). PP242 inhibits global protein synthesis, delays cyclin B accumulation, cyclin B/CDK1 complex activation and consequently entry into the mitotic phase of the cell cycle triggered by fertilization. PP242 inhibits cyclin B mRNA recruitment into active polysomes triggered by fertilization. An amount of cyclin B mRNA present in active polysomes appears to be insensitive to PP242 treatment. Taken together, our results suggest that, following sea urchin egg fertilization, cyclin B mRNA translation is controlled by two independent mechanisms: a PP242-sensitive and an additional PP242-insentitive mechanism.

Published
2016
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9. mTOR Signaling at the Crossroad between Metazoan Regeneration and Human Diseases

Author

Patrick Cormier, Julia Morales, Agnès Boutet, Yasmine Lund-Ricard, Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Station biologique de Roscoff (SBR), and Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
human diseases, muscle, [SDV]Life Sciences [q-bio], Review, lcsh:Chemistry, 0302 clinical medicine, Osteogenesis, Intestinal Mucosa, Axon, lcsh:QH301-705.5, Spectroscopy, axon, 0303 health sciences, Kinase, Stem Cells, TOR Serine-Threonine Kinases, Cell Differentiation, General Medicine, differentiation, Medical research, 3. Good health, Computer Science Applications, Cell biology, medicine.anatomical_structure, mTOR pathway, Disease Susceptibility, Stem cell, Signal Transduction, kidney, autophagy, proliferation, appendage, Biology, liver, Catalysis, Inorganic Chemistry, 03 medical and health sciences, epidermis, medicine, Animals, Humans, Physical and Theoretical Chemistry, Muscle, Skeletal, Molecular Biology, PI3K/AKT/mTOR pathway, 030304 developmental biology, Wound Healing, Mtor signaling, Regeneration (biology), Organic Chemistry, Autophagy, Axons, stem cell, whole-body, lcsh:Biology (General), lcsh:QD1-999, regeneration, Hepatocytes, 030217 neurology & neurosurgery
Abstract

International audience; A major challenge in medical research resides in controlling the molecular processes of tissue regeneration, as organ and structure damage are central to several human diseases. A survey of the literature reveals that mTOR (mechanistic/mammalian target of rapamycin) is involved in a wide range of regeneration mechanisms in the animal kingdom. More particularly, cellular processes such as growth, proliferation, and differentiation are controlled by mTOR. In addition, autophagy, stem cell maintenance or the newly described intermediate quiescence state, G alert , imply upstream monitoring by the mTOR pathway. In this review, we report the role of mTOR signaling in reparative regenerations in different tissues and body parts (e.g., axon, skeletal muscle, liver, epithelia, appendages, kidney, and whole-body), and highlight how the mTOR kinase can be viewed as a therapeutic target to boost organ repair. Studies in this area have focused on modulating the mTOR pathway in various animal models to elucidate its contribution to regeneration. The diversity of metazoan species used to identify the implication of this pathway might then serve applied medicine (in better understanding what is required for efficient treatments in human diseases) but also evolutionary biology. Indeed, species-specific differences in mTOR modulation can contain the keys to appreciate why certain regeneration processes have been lost or conserved in the animal kingdom.

Published
2020
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10. A variant mimicking hyperphosphorylated 4E-BP inhibits protein synthesis in a sea urchin cell-free, cap-dependent translation system.

Author

Nathalie Oulhen, Sandrine Boulben, Michael Bidinosti, Julia Morales, Patrick Cormier, and Bertrand Cosson

Subjects
Medicine, Science
Abstract

BACKGROUND: 4E-BP is a translational inhibitor that binds to eIF4E to repress cap-dependent translation initiation. This critical protein:protein interaction is regulated by the phosphorylation of 4E-BP. Hypophosphorylated 4E-BP binds to eIF4E and inhibits cap-dependent translation, whereas hyperphosphorylated forms do not. While three 4E-BP proteins exist in mammals, only one gene encoding for 4E-BP is present in the sea urchin genome. The protein product has a highly conserved core domain containing the eIF4E-binding domain motif (YxxxxLPhi) and four of the regulatory phosphorylation sites. METHODOLOGY/PRINCIPAL FINDINGS: Using a sea urchin cell-free cap-dependent translation system prepared from fertilized eggs, we provide the first direct evidence that the sea urchin 4E-BP inhibits cap-dependent translation. We show here that a sea urchin 4E-BP variant, mimicking phosphorylation on four core residues required to abrogate binding to eIF4E, surprisingly maintains physical association to eIF4E and inhibits protein synthesis. CONCLUSIONS/SIGNIFICANCE: Here, we examine the involvement of the evolutionarily conserved core domain and phosphorylation sites of sea urchin 4E-BP in the regulation of eIF4E-binding. These studies primarily demonstrate the conserved activity of the 4E-BP translational repressor and the importance of the eIF4E-binding domain in sea urchin. We also show that a variant mimicking hyperphosphorylation of the four regulatory phosphorylation sites common to sea urchin and human 4E-BP is not sufficient for release from eIF4E and translation promotion. Therefore, our results suggest that there are additional mechanisms to that of phosphorylation at the four critical sites of 4E-BP that are required to disrupt binding to eIF4E.

Published
2009
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11. Translational Control of Canonical and Non-Canonical Translation Initiation Factors at the Sea Urchin Egg to Embryo Transition

Author

Patrick Cormier, Héloïse Chassé, Julia Morales, Sandrine Boulben, Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Station biologique de Roscoff (SBR), and Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Male, Embryo, Nonmammalian, Zygote, Heterogeneous-Nuclear Ribonucleoproteins, lcsh:Chemistry, chemistry.chemical_compound, sea urchin fertilization, initiation complex, 0302 clinical medicine, Translational regulation, EIF4B, Eukaryotic Initiation Factors, Peptide Chain Initiation, Translational, lcsh:QH301-705.5, Spectroscopy, 0303 health sciences, EIF4G, TOR Serine-Threonine Kinases, EIF4E, translational control, Translation (biology), General Medicine, Computer Science Applications, Cell biology, mTOR pathway, Female, Signal Transduction, Biology, Catalysis, Article, Inorganic Chemistry, 03 medical and health sciences, Eukaryotic translation, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Initiation factor, Animals, RNA, Messenger, Physical and Theoretical Chemistry, Molecular Biology, 030304 developmental biology, Organic Chemistry, Eukaryotic Initiation Factor-4E, [SDV.BDD.EO]Life Sciences [q-bio]/Development Biology/Embryology and Organogenesis, chemistry, lcsh:Biology (General), lcsh:QD1-999, eIF4A, Fertilization, Polyribosomes, Sea Urchins, eIF4E, Eukaryotic Initiation Factor-4A, Eukaryotic Initiation Factor-4G, 030217 neurology & neurosurgery
Abstract

International audience; Sea urchin early development is a powerful model to study translational regulation under physiological conditions. Fertilization triggers an activation of the translation machinery responsible for the increase of protein synthesis necessary for the completion of the first embryonic cell cycles. The cap-binding protein eIF4E, the helicase eIF4A and the large scaffolding protein eIF4G are assembled upon fertilization to form an initiation complex on mRNAs involved in cap-dependent translation initiation. The presence of these proteins in unfertilized and fertilized eggs has already been demonstrated, however data concerning the translational status of translation factors are still scarce. Using polysome fractionation, we analyzed the impact of fertilization on the recruitment of mRNAs encoding initiation factors. Strikingly, whereas the mRNAs coding eIF4E, eIF4A, and eIF4G were not recruited into polysomes at 1 h post-fertilization, mRNAs for eIF4B and for non-canonical initiation factors such as DAP5, eIF4E2, eIF4E3, or hnRNP Q, are recruited and are differentially sensitive to the activation state of the mechanistic target of rapamycin (mTOR) pathway. We discuss our results suggesting alternative translation initiation in the context of the early development of sea urchins.

Published
2019
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12. MAPK/ERK activity is required for the successful progression of mitosis in sea urchin embryos

Author

Julia Morales, Héloïse Chassé, Odile Mulner-Lorillon, Patrick Cormier, Robert Bellé, Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Station biologique de Roscoff [Roscoff] (SBR), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
DNA Replication, 0301 basic medicine, MAPK/ERK pathway, Embryo, Nonmammalian, Cell cycle checkpoint, MAP Kinase Signaling System, Cyclin B, Mitosis, Microtubules, 03 medical and health sciences, 0302 clinical medicine, CDC2 Protein Kinase, Nitriles, Butadienes, Animals, Phosphorylation, [SDV.BDD]Life Sciences [q-bio]/Development Biology, Molecular Biology, Ovum, Cyclin-dependent kinase 1, biology, embryonic cell division, Cell Biology, Cell cycle, Biological Evolution, Chromatin, Cell biology, Enzyme Activation, Spindle checkpoint, 030104 developmental biology, Fertilization, Protein Biosynthesis, Sea Urchins, 030220 oncology & carcinogenesis, biology.protein, cell cycle checkpoint, Carrier Proteins, Cell Division, Developmental Biology
Abstract

International audience; Using sea urchin embryos, we demonstrate that the MEK/MAPK/ERK cascade is essential for the proper progression of the cell cycle. Activation of a limited fraction of MAPK/ERK is required between S-phase and M-phase. Neither DNA replication nor CDK1 activation are impacted by the inhibition of this small active MAPK/ERK fraction. Nonetheless, the chromatin and spindle organisations are profoundly altered. Early morphological disorders induced by the absence of MAPK/ERK activation are correlated with an important inhibition of global protein synthesis and modification in the cyclin B accumulation profile. After appearance of morphological disorders, there is an increase in the level of the inhibitor of protein synthesis, 4E-BP, and, ultimately, an activation of the spindle checkpoint. Altogether, our results suggest that MAPK/ERK activity is required for the synthesis of (a) protein(s) implicated in an early step of chromatin /microtubule attachment. If this MAPK/ERK-dependent step is not achieved, the cell activates a new checkpoint mechanism, involving the reappearance of 4E-BP that maintains a low level of protein translation, thus saving cellular energy.

Published
2017
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13. Model of the delayed translation of cyclin B maternal mRNA after sea urchin fertilization

Author

Odile Mulner-Lorillon, Julia Morales, Anne Siegel, Robert Bellé, Patrick Cormier, Jérémie Bourdon, and Vincent Picard

Subjects
0301 basic medicine, Messenger RNA, education.field_of_study, biology, Population, Cyclin A, Cyclin B, Translation (biology), Cell Biology, 03 medical and health sciences, chemistry.chemical_compound, 030104 developmental biology, 0302 clinical medicine, Biochemistry, Biosynthesis, chemistry, biology.animal, Genetics, Protein biosynthesis, biology.protein, education, Sea urchin, 030217 neurology & neurosurgery, Developmental Biology
Abstract

Sea urchin eggs exhibit a cap-dependent increase in protein synthesis within minutes after fertilization. This rise in protein synthesis occurs at a constant rate for a great number of proteins translated from the different available mRNAs. Surprisingly, we found that cyclin B, a major cell-cycle regulator, follows a synthesis pattern that is distinct from the global protein population, so we developed a mathematical model to analyze this dissimilarity in biosynthesis kinetic patterns. The model includes two pathways for cyclin B mRNA entry into the translational machinery: one from immediately available mRNA (mRNAcyclinB) and one from mRNA activated solely after fertilization (XXmRNAcyclinB). Two coefficients, α and β, were added to fit the measured scales of global protein and cyclin B synthesis, respectively. The model was simplified to identify the synthesis parameters and to allow its simulation. The calculated parameters for activation of the specific cyclin B synthesis pathway after fertilization included a kinetic constant (ka ) of 0.024 sec-1 , for the activation of XXmRNAcyclinB, and a critical time interval (t2 ) of 42 min. The proportion of XXmRNAcyclinB form was also calculated to be largely dominant over the mRNAcyclinB form. Regulation of cyclin B biosynthesis is an example of a select protein whose translation is controlled by pathways that are distinct from housekeeping proteins, even though both involve the same cap-dependent initiation pathway. Therefore, this model should help provide insight to the signaling utilized for the biosynthesis of cyclin B and other select proteins. Mol. Reprod. Dev. 83: 1070-1082, 2016. © 2016 Wiley Periodicals, Inc.

Published
2016
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14. In vivo analysis of protein translation activity in sea urchin eggs and embryos

Author

Patrick Cormier, Julia Morales, Héloïse Chassé, Virginie Glippa, Florian Pontheaux, Sandrine Boulben, Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS), Sorbonne Université (SU), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Station biologique de Roscoff (SBR), and Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0303 health sciences, Messenger RNA, biology, [SDV]Life Sciences [q-bio], Embryo, Cell biology, 03 medical and health sciences, In vivo, biology.animal, Polysome, Gene expression, Protein biosynthesis, Luciferase, Sea urchin, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology
Abstract

Protein synthesis is a major regulatory step of gene expression in different physiological processes including development. Translation of proteins in sea urchin is stimulated upon fertilization and is necessary for cell cycle progression and development. Translational control is exerted through multifactorial mechanisms, including mRNA recruitment into polysomes and increased rates of translational activity. In this chapter, we review the methods used in sea urchin eggs and embryos to analyze translation activity in vivo both from perspectives of the proteins and of the mRNAs. First, we describe methods to quantify or visualize newly synthesized proteins with radioactive and non-radioactive labeling techniques. Next we present the polysome isolation and profiling on sucrose gradients, allowing the identification of translated mRNAs. Finally, we outline a procedure to follow the translation of a reporter luciferase protein from an mRNA microinjected into the egg.

Published
2019
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15. Folate-conjugated stealth archaeosomes for the targeted delivery of novel antitumoral peptides

Author

Thierry Benvegnu, Julie Barbeau, Ahmad Jiblaoui, Thomas Vives, Virginie Glippa, Patrick Cormier, Bertrand Cosson, Institut des Sciences Chimiques de Rennes (ISCR), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA), Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), and Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Nano-carriers, General Chemical Engineering, Peptide, Folate ligands, 02 engineering and technology, Tumor cells, 010402 general chemistry, 01 natural sciences, [CHIM]Chemical Sciences, chemistry.chemical_classification, Folate receptor, Vesicle, General Chemistry, 021001 nanoscience & nanotechnology, Ligand (biochemistry), Lipids, In vitro, 0104 chemical sciences, Amino acid, Cell membranes, Anticancer activities, chemistry, Biochemistry, Targeted drug delivery, Site-specific, Drug-targeting, Targeted delivery, Nanocarriers, Peptides, 0210 nano-technology
Abstract

International audience; In this work, novel archaeosomes based on Egg-PC and a mixture of PEGylated archaeal tetraether lipids were investigated as nanocarriers for in vitro delivery of an original anticancer peptide. With the aim to develop site-specific drug targeting, a tetraether equipped with a folate ligand at the PEG5000 terminal end (FA-PEG5000-tetraether) was synthesized in order to bind to folate receptors (over)expressed on the tumor cell surfaces. The original peptide A1 and its inactive analogue A1Yala (17 amino acids) were encapsulated into Egg-PC vesicles incorporating FA-PEG5000-tetraether and/or PEG2000-tetraether lipids in order to evaluate the in vitro anticancer activity of A1-loaded archaeosomes. Results showed a particular behaviour when A1 was encapsulated into the folate-equipped archaeosomes particularly during the first hour of incubation. © The Royal Society of Chemistry 2016.

Published
2016
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16. Analysis of translation using polysome profiling

Author

Sandrine Boulben, Julia Morales, Patrick Cormier, Vlad Costache, Héloïse Chassé, Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Station biologique de Roscoff [Roscoff] (SBR), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, Male, [SDV]Life Sciences [q-bio], ved/biology.organism_classification_rank.species, Gene regulatory network, Computational biology, Biology, polysome profiling, translation regulation, sea urchin, 03 medical and health sciences, 0302 clinical medicine, Polysome, Translational regulation, Gene expression, Genetics, Protein biosynthesis, Animals, RNA, Messenger, Model organism, ved/biology, Sequence Analysis, RNA, Gene Expression Profiling, High-Throughput Nucleotide Sequencing, Translation (biology), Molecular biology, Gene expression profiling, 030104 developmental biology, fertilization, Polyribosomes, Protein Biosynthesis, Paracentrotus, Methods Online, Female, polysome, 030217 neurology & neurosurgery
Abstract

International audience; During the past decade, there has been growing interest in the role of translational regulation of gene expression in many organisms. Polysome profiling has been developed to infer the translational status of a specific mRNA species or to analyze the trans-latome, i.e. the subset of mRNAs actively translated in a cell. Polysome profiling is especially suitable for emergent model organisms for which genomic data are limited. In this paper, we describe an optimized protocol for the purification of sea urchin polysomes and highlight the critical steps involved in polysome purification. We applied this protocol to obtain experimental results on translational regulation of mR-NAs following fertilization. Our protocol should prove useful for integrating the study of the role of transla-tional regulation in gene regulatory networks in any biological model. In addition, we demonstrate how to carry out high-throughput processing of polysome gradient fractions, for the simultaneous screening of multiple biological conditions and large-scale preparation of samples for next-generation sequencing.

Published
2017
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17. The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS

Author

Nathalie Oulhen, Murielle Jam, Justyna Ronzca, Mirjam Czjzek, Bertrand Cosson, Pauline Gosselin, Patrick Cormier, Mer et santé (MS), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), Végétaux marins et biomolécules, Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-GOEMAR-Centre National de la Recherche Scientifique (CNRS), Université européenne de Bretagne - European University of Brittany (UEB), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Models, Molecular, Eukaryotic Initiation Factor-4E, Plasma protein binding, Biology, regulation of translation, 03 medical and health sciences, 0302 clinical medicine, X-Ray Diffraction, Structural Biology, Sequence Analysis, Protein, Eukaryotic initiation factor, Scattering, Small Angle, Bound state, Genetics, Initiation factor, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Eukaryotic Initiation Factors, 030304 developmental biology, 0303 health sciences, Small-angle X-ray scattering, EIF4E, E-BP compaction, Translation (biology), SAXS, Molecular biology, 3. Good health, eIF4E, fuzzy complex, Biophysics, 030217 neurology & neurosurgery, Protein Binding
Abstract

International audience; eIF4E binding protein (4E-BP) inhibits translation of capped mRNA by binding to the initiation factor eIF4E and is known to be mostly or completely unstructured in both free and bound states. Using small angle X-ray scattering (SAXS), we report here the analysis of 4E-BP structure in solution, which reveals that while 4E-BP is intrinsically disordered in the free state, it undergoes a dramatic compaction in the bound state. Our results demonstrate that 4E-BP and eIF4E form a 'fuzzy complex', challenging current visions of eIF4E/4E-BP complex regulation.

Published
2010
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18. Sea urchin embryo as a model for analysis of the signaling pathways linking DNA damage checkpoint, DNA repair and apoptosis

Author

Odile Mulner-Lorillon, R. Le Bouffant, Patrick Cormier, Robert Bellé, A. Cueff, Mer et santé (MS), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)

Subjects
MESH: Signal Transduction, Embryo, Nonmammalian, Cell cycle checkpoint, DNA Repair, Cyclin B, Apoptosis, MESH: Animals, MESH: DNA Repair, 0303 health sciences, MESH: Kinetics, biology, 030302 biochemistry & molecular biology, Cell cycle, MESH: CDC2 Protein Kinase, 3. Good health, Cell biology, Caspases, embryonic structures, MESH: Cell Division, Molecular Medicine, Cell Division, Signal Transduction, MESH: Enzyme Activation, animal structures, DNA damage, DNA repair, Models, Biological, 03 medical and health sciences, Cellular and Molecular Neuroscience, MESH: Mutagens, CDC2 Protein Kinase, Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, CHEK1, Molecular Biology, 030304 developmental biology, MESH: DNA Damage, Pharmacology, DNA integrity checkpoint, MESH: Caspases, MESH: Apoptosis, MESH: Models, Biological, MESH: Embryo, Nonmammalian, MESH: Cyclin B, Cell Biology, G2-M DNA damage checkpoint, MESH: Sea Urchins, Enzyme Activation, Kinetics, Sea Urchins, biology.protein, DNA Damage, Mutagens
Abstract

International audience; DNA integrity checkpoint control was studied in the sea urchin early embryo. Treatment of the embryos with genotoxic agents such as methyl methanesulfonate (MMS) or bleomycin induced the activation of a cell cycle checkpoint as evidenced by the occurrence of a delay or an arrest in the division of the embryos and an inhibition of CDK1/cyclin B activating dephosphorylation. The genotoxic treatment was shown to induce DNA damage that depended on the genotoxic concentration and was correlated with the observed cell cycle delay. At low genotoxic concentrations, embryos were able to repair the DNA damage and recover from checkpoint arrest, whereas at high doses they underwent morphological and biochemical changes characteristic of apoptosis. Finally, extracts prepared from embryos were found to be capable of supporting DNA repair in vitro upon incubation with oligonucleotides mimicking damage. Taken together, our results demonstrate that sea urchin early embryos contain fully functional and activatable DNA damage checkpoints. Sea urchin embryos are discussed as a promising model to study the signaling pathways of cell cycle checkpoint, DNA repair and apoptosis, which upon deregulation play a significant role in the origin of cancer.

Published
2007
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19. Translational control genes in the sea urchin genome

Author

Patrick Cormier, Bertrand Cosson, Odile Mulner-Lorillon, Julia Morales, Wendy S. Beane, Robert Bellé, Emmanuelle Morin, Cynthia A. Bradham, Mer et santé (MS), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), Department of Geography, Department of geography, Laboratoire d'Informatique de Nantes Atlantique (LINA), Mines Nantes (Mines Nantes)-Université de Nantes (UN)-Centre National de la Recherche Scientifique (CNRS), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Sea urchin, MESH: Sequence Homology, Amino Acid, Peptide Chain Elongation, Translational, MESH: Cell Cycle, MESH: Amino Acid Sequence, Genome, chemistry.chemical_compound, 0302 clinical medicine, MESH: Reverse Transcriptase Polymerase Chain Reaction, Cap-dependent initiation, MESH: Animals, MESH: Proteins, Peptide Chain Initiation, Translational, Conserved Sequence, Genetics, 0303 health sciences, MESH: Conserved Sequence, biology, EIF4G, Reverse Transcriptase Polymerase Chain Reaction, EIF4E, Cell Cycle, Cell Differentiation, MESH: Gene Expression Regulation, MESH: Protein Biosynthesis, Elongation factors, MESH: Cell Differentiation, MESH: Peptide Chain Initiation, Translational, In silico, Molecular Sequence Data, MESH: Sequence Alignment, 03 medical and health sciences, biology.animal, Animals, MESH: Genome, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, Gene, Molecular Biology, MESH: Peptide Chain Elongation, Translational, 030304 developmental biology, MESH: Molecular Sequence Data, Sequence Homology, Amino Acid, Proteins, Translational control, Cell Biology, MESH: Sea Urchins, Elongation factor, chemistry, Gene Expression Regulation, Protein Biosynthesis, Sea Urchins, Human genome, Sequence Alignment, 030217 neurology & neurosurgery, Developmental Biology
Abstract

International audience; Sea urchin eggs and early cleavage stage embryos provide an example of regulated gene expression at the level of translation. The availability of the sea urchin genome offers the opportunity to investigate the "translational control" toolkit of this model system. The annotation of the genome reveals that most of the factors implicated in translational control are encoded by nonredundant genes in echinoderm, an advantage for future functional studies. In this paper, we focus on translation factors that have been shown or suggested to play crucial role in cell cycle and development of sea urchin embryos. Addressing the cap-binding translational control, three closely related eIF4E genes (class I, II, III) are present, whereas its repressor 4E-BP and its activator eIF4G are both encoded by one gene. Analysis of the class III eIF4E proteins in various phyla shows an echinoderm-specific amino acid substitution. Furthermore, an interaction site between eIF4G and poly(A)-binding protein is uncovered in the sea urchin eIF4G proteins and is conserved in metazoan evolution. In silico screening of the sea urchin genome has uncovered potential new regulators of eIF4E sharing the common eIF4E recognition motif. Taking together, these data provide new insights regarding the strong requirement of cap-dependent translation following fertilization. The genome analysis gives insights on the complexity of eEF1B structure and motifs of functional relevance, involved in the translational control of gene expression at the level of elongation. Finally, because deregulation of translation process can lead to diseases and tumor formation in humans, the sea urchin orthologs of human genes implicated in human diseases and signaling pathways regulating translation were also discussed.

Published
2006
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20. The genomic repertoire for cell cycle control and DNA metabolism in S. purpuratus

Author

Julia Morales, James A. Coffman, Bertrand Cosson, Anthony J. Robertson, William F. Marzluff, Anne Marie Genevière, Antoine Aze, Cynthia A. Bradham, Patrick Cormier, Nikki L. Adams, Odile Mulner-Lorillon, Antonio Fernandez-Guerra, Mer et santé (MS), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), Antarctic Climate and Ecosystems Cooperative Research Centre (ACE-CRC), Institute of Aerodynamics and Fluid Mechanics (AER), Technische Universität Munchen - Université Technique de Munich [Munich, Allemagne] (TUM), International Research Institute for Climate and Society (IRI), Earth Institute at Columbia University, Columbia University [New York]-Columbia University [New York], Soils Group, Macaulay Institute, Department of Haematology, University of Cambridge [UK] (CAM), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Sea urchin, MESH: Sequence Homology, Amino Acid, MESH: Cell Cycle, MESH: Amino Acid Sequence, Genome, Conserved sequence, 0302 clinical medicine, MESH: Animals, MESH: Phylogeny, Conserved Sequence, Phylogeny, Genetics, 0303 health sciences, MESH: Conserved Sequence, biology, Checkpoint, Cell Cycle, MESH: DNA, Cell cycle, Cyclin-Dependent Kinases, Cell biology, MESH: Cyclin-Dependent Kinases, 030220 oncology & carcinogenesis, embryonic structures, DNA repair, Molecular Sequence Data, MESH: Sequence Alignment, Replication, Mitosis, Kinases, 03 medical and health sciences, Cyclin-dependent kinase, Animals, MESH: Genome, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, 14. Life underwater, Amino Acid Sequence, Gene, MESH: Protein Kinases, Molecular Biology, 030304 developmental biology, MESH: Molecular Sequence Data, Sequence Homology, Amino Acid, DNA replication, DNA, Cell Biology, biology.organism_classification, Strongylocentrotus purpuratus, MESH: Sea Urchins, Sea Urchins, biology.protein, Protein Kinases, Sequence Alignment, Developmental Biology
Abstract

International audience; A search of the Strongylocentrotus purpuratus genome for genes associated with cell cycle control and DNA metabolism shows that the known repertoire of these genes is conserved in the sea urchin, although with fewer family members represented than in vertebrates, and with some cases of echinoderm-specific gene diversifications. For example, while homologues of the known cyclins are mostly encoded by single genes in S. purpuratus (unlike vertebrates, which have multiple isoforms), there are additional genes encoding novel cyclins of the B and K/L types. Almost all known cyclin-dependent kinases (CDKs) or CDK-like proteins have an orthologue in S. purpuratus; CDK3 is one exception, whereas CDK4 and 6 are represented by a single homologue, referred to as CDK4. While the complexity of the two families of mitotic kinases, Polo and Aurora, is close to that found in the nematode, the diversity of the NIMA-related kinases (NEK proteins) approaches that of vertebrates. Among the nine NEK proteins found in S. purpuratus, eight could be assigned orthologues in vertebrates, whereas the ninth is unique to sea urchins. Most known DNA replication, DNA repair and mitotic checkpoint genes are also present, as are homologues of the pRB (two) and p53 (one) tumor suppressors. Interestingly, the p21/p27 family of CDK inhibitors is represented by one homologue, whereas the INK4 and ARF families of tumor suppressors appear to be absent, suggesting that these evolved only in vertebrates. Our results suggest that, while the cell cycle control mechanisms known from other animals are generally conserved in sea urchin, parts of the machinery have diversified within the echinoderm lineage. The set of genes uncovered in this analysis of the S. purpuratus genome should enhance future research on cell cycle control and developmental regulation in this model.

Published
2006
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21. eIF4E et étapes décisionnelles du développement embryonnaire

Author

Patrick Cormier and Nathalie Oulhen

Subjects
General Medicine, Biology, Molecular biology, General Biochemistry, Genetics and Molecular Biology
Abstract

La synthèse protéique représente une étape importante de l’expression des gènes. Au cours du développement embryonnaire, la traduction des ARNm n’est pas toujours systématique, et résulte d’un contrôle efficace permettant l’expression de la protéine au bon moment et au bon endroit dans l’embryon. Les facteurs d’initiation (eIF, eukaryotic initiation factors) sont des acteurs clés du contrôle de la synthèse protéique. Parmi eux, le facteur eIF4E, par le biais d’associations avec différents partenaires, joue un rôle majeur qui se répercute depuis la gamétogenèse et la fécondation jusqu’à l’établissement des axes embryonnaires. Cet article se concentre sur le rôle d’eIF4E dans le contrôle de la régulation de la synthèse protéique en amont des décisions développementales. Les exemples sélectionnés illustrent l’importance du contrôle traductionnel en général, et au cours du développement embryonnaire en particulier. La découverte de mécanismes, parfois très sophistiqués, qui contrôlent la traduction des ARNm au cours du développement conduit le biologiste à porter un regard nouveau sur cette étape de la régulation de l’expression des gènes., Regulation of mRNA translation is an important regulatory step in gene expression. During embryonic development, mRNA translation is tightly regulated to produce the protein at the right place, at the right time. The eukaryotic initiation factor 4E (eIF4E) is a major target for the regulation of cap-dependent translation, that plays a key role during embryogenesis including gametogenesis, fertilization and establishment of embryonic axes. In this review, we describe recent advances illustrating the importance of the translational regulator eIF4E and its partners in developmental decisions.

Published
2006
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22. Embryonic-stage-dependent changes in the level of eIF4E-binding proteins during early development of sea urchin embryos

Author

Patrick Salaun, Sandrine Boulben, Julia Morales, Patrick Cormier, Odile Mulner-Lorillon, Nahum Sonenberg, and Robert Bellé

Subjects
Embryo, Nonmammalian, Eukaryotic Initiation Factor-4E, Embryogenesis, EIF4E, Embryonic Development, Embryonic Stage, Cell Biology, Biology, Up-Regulation, Cell biology, Molecular Weight, Human fertilization, Eukaryotic translation, Fertilization, Sea Urchins, biology.animal, Botany, Animals, RNA, Messenger, Carrier Proteins, Mitosis, Sea urchin
Abstract

The eukaryotic initiation factor 4E (eIF4E)-binding proteins (4E-BPs) inhibit translation initiation by binding eIF4E and preventing recruitment of the translation machinery to mRNA. We have previously shown that fertilization of sea urchin eggs triggers eIF4E–4E-BP complex dissociation and 4E-BP degradation. Here, we show that microinjection of eIF4E-binding motif peptide into unfertilized eggs delays the onset of the first mitosis triggered by fertilization, demonstrating that dissociation of the eIF4E–4E-BP complex is functionally important for the first mitotic division in sea urchin embryos. We also show by gel filtration analyses that eIF4E is present in unfertilized eggs as an 80 kDa molecular mass complex containing 4E-BP and a new 4E-BP of 40 kDa. Fertilization triggers the dissociation of eIF4E from these two 4E-BPs and triggers the rapid recruitment of eIF4E into a high-molecular-mass complex. Release of eIF4E from the two 4E-BPs is correlated with a decrease in the total level of both 4E-BPs following fertilization. Abundance of the two 4E-BPs has been monitored during embryonic development. The level of the two proteins remains very low during the rapid cleavage stage of early development and increases 8 hours after fertilization. These results demonstrate that these two 4E-BPs are down- and upregulated during the embryonic development of sea urchins. Consequently, these data suggest that eIF4E availability to other partners represents an important determinant of the early development of sea urchin embryos.

Published
2005
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23. Formulated Glyphosate Activates the DNA-Response Checkpoint of the Cell Cycle Leading to the Prevention of G2/M Transition

Author

Robert Bellé, Julia Morales, Patrick Cormier, Odile Mulner-Lorillon, and Julie Marc

Subjects
G2 Phase, Embryo, Nonmammalian, Cell cycle checkpoint, Cdc25, Chemistry, Pharmaceutical, Blotting, Western, Cyclin A, Glycine, Cyclin B, Toxicology, CDC2 Protein Kinase, Animals, CHEK1, S phase, Ovum, Cyclin-dependent kinase 1, biology, Herbicides, Cell Cycle, DNA, Cell cycle, Phosphoric Monoester Hydrolases, Cell biology, Biochemistry, Depression, Chemical, Sea Urchins, biology.protein, Cell Division
Abstract

A glyphosate containing pesticide impedes at 10 mM glyphosate the G2/M transition as judged from analysis of the first cell cycle of sea urchin development. We show that formulated glyphosate prevented dephosphorylation of Tyr 15 of the cell cycle regulator CDK1/cyclin B in vivo, the end point target of the G2/M cell cycle checkpoint. Formulated glyphosate had no direct effect on the dual specific cdc25 phosphatase activity responsible for Tyr 15 dephosphorylation. At a concentration that efficiently impeded the cell cycle, formulated glyphosate inhibited the synthesis of DNA occurring in S phase of the cell cycle. The extent of the inhibition of DNA synthesis by formulated glyphosate was correlated with the effect on the cell cycle. We conclude that formulated glyphosate's effect on the cell cycle is exerted at the level of the DNA-response checkpoint of S phase. The resulting inhibition of CDK1/cyclin B Tyr 15 dephosphorylation leads to prevention of the G2/M transition and cell cycle progression.

Published
2004
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24. Sea urchin elongation factor 1? (EF1?) and evidence for cell cycle-directed localization changes of a sub-fraction of the protein at M phase

Author

M. Le Breton, Julia Morales, Sandrine Boulben, Patrick Cormier, Robert Bellé, A. Monnier, and Odile Mulner-Lorillon

Subjects
Cell division, Molecular Sequence Data, Cyclin B, Mitosis, Cellular and Molecular Neuroscience, Peptide Elongation Factor 1, Tubulin, biology.animal, Animals, Amino Acid Sequence, Molecular Biology, Sea urchin, Pharmacology, Cyclin-dependent kinase 1, biology, Cell Cycle, Cell Biology, Cell cycle, Molecular biology, Eukaryotic translation elongation factor 1 alpha 1, Spindle apparatus, Cell biology, Elongation factor, Protein Transport, Sea Urchins, biology.protein, Molecular Medicine
Abstract

Eukaryotic elongation factor 1 (eEF1) is a translational multimolecular complex reported in higher eukaryotes to be a target of CDK1/cyclin B, the universal regulator of M phase, but whose role in the cell cycle remains to be determined. A specific polyclonal antibody was produced and used to characterize the delta subunit of sea urchin elongation factor 1 (SgEF1delta) in early embryos, a powerful model for investigating cell cycle regulation. The SgEF1delta protein was present in unfertilized eggs as two isoforms of 35 and 37 kDa, issued from two different mRNAs. The two canonical eEF1delta partners, eEF1gamma and eEF1beta, were shown to co-immunoprecipitate with the SgEF1delta isoforms. Both isoforms were associated in a macromolecular complex, which resolved upon gel filtration chromatography at a molecular weight400 kDa, suggesting association with other yet unidentified partners. After fertilization, the amount as well as the ratio of both SgEF1delta isoforms remained constant during the first cell division as judged by Western blotting. Immunofluorescence analysis showed that a pool of the protein concentrated as a ring at the embryo nuclear location around the period of nuclear envelope breakdown and was visualized later as two large spheres around the mitotic spindle poles. Thus, the eEF1delta protein shows cell cycle-specific localization changes in sea urchin embryos.

Published
2003
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25. EIF4E/4E-BP dissociation and 4E-BP degradation in the first mitotic division of the sea urchin embryo

Author

Patrick Salaün, Julia Morales, Robert Bellé, Patrick Cormier, S.téphane Pyronnet, Odile Mulner-Lorillon, and Nahum Sonenberg

Subjects
Male, Proteolysis, Cyclin B, Mitosis, 4E-BP, Eukaryotic translation, biology.animal, CDC2 Protein Kinase, Protein biosynthesis, medicine, Animals, Initiation factor, Sea urchin, Molecular Biology, Sirolimus, biology, medicine.diagnostic_test, EIF4E, Cell Biology, Phosphoproteins, Eukaryotic Initiation Factor-4E, Biochemistry, 4E-BP degradation, Sea Urchins, eIF4E, Fertilization, biology.protein, Female, Carrier Proteins, Developmental Biology
Abstract

The mRNA’s cap-binding protein eukaryotic translation initiation factor (eIF)4E is a major target for the regulation of translation initiation. eIF4E activity is controlled by a family of translation inhibitors, the eIF4E-binding proteins (4E-BPs). We have previously shown that a rapid dissociation of 4E-BP from eIF4E is related with the dramatic rise in protein synthesis that occurs following sea urchin fertilization. Here, we demonstrate that 4E-BP is destroyed shortly following fertilization and that 4E-BP degradation is sensitive to rapamycin, suggesting that proteolysis could be a novel means of regulating 4E-BP function. We also show that eIF4E/4E-BP dissociation following fertilization is sensitive to rapamycin. Furthermore, while rapamycin modestly affects global translation rates, the drug strongly inhibits cyclin B de novo synthesis and, consequently, precludes the completion of the first mitotic cleavage. These results demonstrate that, following sea urchin fertilization, cyclin B translation, and thus the onset of mitosis, are regulated by a rapamycin-sensitive pathway. These processes are effected at least in part through eIF4E/4E-BP complex dissociation and 4E-BP degradation.

Published
2003
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26. An eIF4E-interacting peptide induces cell death in cancer cell lines

Author

I Gauffeny, Bertrand Cosson, Virginie Glippa, C Berthou, Mirjam Czjzek, R Le Bloas, H Saad, M Masse, Patrick Cormier, Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université européenne de Bretagne - European University of Brittany (UEB), Department of Clinical Hematology, Institute of Cancerology and Hematology, Centre Hospitalier Régional Universitaire de Brest (CHRU Brest), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Station biologique de Roscoff [Roscoff] (SBR), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Cancer Research, Programmed cell death, Cell Membrane Permeability, Eukaryotic Initiation Factor-4E, Immunology, Peptide, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Cell Membrane Structures, Cellular and Molecular Neuroscience, Necrosis, Eukaryotic translation, Eukaryotic initiation factor, Cell Line, Tumor, Neoplasms, Animals, Humans, Actin, chemistry.chemical_classification, Cell Death, Protein Stability, EIF4E, Cell Biology, Actins, 3. Good health, Cell biology, chemistry, Cell culture, Protein Biosynthesis, Original Article, Rabbits, Peptides, Protein Binding
Abstract

The eukaryotic initiation factor eIF4E is essential for cap-dependent initiation of translation in eukaryotes. Abnormal regulation of eIF4E has been implicated in oncogenic transformation. We developed an eIF4E-binding peptide derived from Angel1, a partner of eIF4E that we recently identified. We show here that this peptide fused to a penetratin motif causes drastic and rapid cell death in several epithelial cancer cell lines. This necrotic cell death was characterized by a drop in ATP levels with F-actin network injury being a key step in extensive plasma membrane blebbing and membrane permeabilization. This synthetic eIF4E-binding peptide provides a candidate pharmacophore for a promising new cancer therapy strategy.

Published
2014
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27. eIF4E Association with 4E-BP Decreases Rapidly Following Fertilization in Sea Urchin

Author

Julia Morales, Odile Mulner-Lorillon, Nahum Sonenberg, Robert Bellé, Stéphane Pyronnet, and Patrick Cormier

Subjects
Male, protein synthesis, 4E-BP, Biology, eIF-4E, sea urchin fertilization, chemistry.chemical_compound, Eukaryotic translation, Peptide Initiation Factors, biology.animal, Protein biosynthesis, Initiation factor, Animals, RNA, Messenger, Phosphorylation, Peptide Chain Initiation, Translational, Sea urchin, Molecular Biology, Ovum, Messenger RNA, EIF4G, Binding protein, EIF4E, Cell Biology, Molecular biology, Precipitin Tests, Cell biology, Eukaryotic Initiation Factor-4E, chemistry, Fertilization, Protein Biosynthesis, Sea Urchins, Female, Carrier Proteins, Ribosomes, Developmental Biology
Abstract

The eukaryotic translation initiation factor (eIF) 4F facilitates the recruitment of ribosomes to the mRNA 5′ end. The 4E-BPs are small proteins with hypophosphorylated forms that interact with the cap binding protein eIF4E, preventing its interaction with eIF4G, thereby preventing ribosome interaction with mRNA. In sea urchin, fertilization triggers a rapid rise in protein synthesis. Here, we demonstrate that a 4E-BP homologue exists and is associated with eIF4E in unfertilized eggs. We also show that 4E-BP/eIF4E association diminishes a few minutes following fertilization. This decrease is correlated with a decrease in the total amount of 4E-BP in combination with an increase in the phosphorylation of the protein. We propose that 4E-BP acts as a repressor of protein synthesis in unfertilized sea urchin eggs and that 4E-BP/eIF4E dissociation plays an important role in the rise in protein synthesis that occurs shortly following fertilization.

Published
2001
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28. Multiple Phosphorylation Sites and Quaternary Organization of Guanine-Nucleotide Exchange Complex of Elongation Factor-1 (EF-1βγδ/ValRS) Control the Various Functions of EF-1α

Author

Robert Bellé, Odile Mulner-Lorillon, Guillaume Bec, Patrick Cormier, and Odile Minella

Subjects
Models, Molecular, Binding Sites, biology, MAP kinase kinase kinase, Protein Conformation, Cyclin-dependent kinase 2, Biophysics, Proteins, Cell Biology, Mitogen-activated protein kinase kinase, Peptide Elongation Factors, Biochemistry, Cell biology, Peptide Elongation Factor 1, biology.protein, Cyclin-dependent kinase complex, Guanine Nucleotide Exchange Factors, Cyclin-dependent kinase 9, Protein phosphorylation, Phosphorylation, Casein kinase 2, Protein kinase A, Molecular Biology
Abstract

The eukaryotic guanine-nucleotide exchange factor commonly called elongation factor-1 betagammadelta (EF-1betagammadelta), comprises four different subunits including valyl-tRNA synthetase (EF-1betagammadelta/ValRS). The factor is multiply-phosphorylated by three different protein kinases, protein kinase C, casein kinase II and cyclin dependent kinase 1 (CDKI). EF-1betagammadelta/ValRS is organized as a macromolecular complex for which we propose a new structural model. Evidence that EF-1betagammadelta/ValRS is a sophisticated supramolecular complex containing many phosphorylation sites, makes it a potential regulator of any of the functions of its partner EF-1alpha, not only involved in protein synthesis elongation, but also in many other cellular functions.

Published
1998
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29. Tracking a refined eIF4E-binding motif reveals Angel1 as a new partner of eIF4E

Author

Stephane Pyronnet, Isabelle Gauffeny, Pauline Gosselin, Virginie Glippa, Yvan Martineau, Bertrand Cosson, Patrick Cormier, Mirjam Czjzek, Gildas Le Corguillé, Julia Morales, Emmanuelle Morin, Mer et santé (MS), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Institut de médecine moléculaire de Rangueil (I2MR), Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)- Institut Fédératif de Recherche Bio-médicale Institution (IFR150)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Végétaux marins et biomolécules, Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-GOEMAR-Centre National de la Recherche Scientifique (CNRS), Chimie Et Interdisciplinarité : Synthèse, Analyse, Modélisation (CEISAM), Université de Nantes - UFR des Sciences et des Techniques (UN UFR ST), Université de Nantes (UN)-Université de Nantes (UN)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Lbi2m, Hal, Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées- Institut Fédératif de Recherche Bio-médicale Institution (IFR150)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-IFR150-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), and Université de Nantes (UN)-Université de Nantes (UN)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)

Subjects
MESH: Ribonucleases, Cytoplasm, Immunoprecipitation, In silico, [SDV]Life Sciences [q-bio], Golgi Apparatus, MESH: Carrier Proteins, Computational biology, Biology, Endoplasmic Reticulum, Mice, 03 medical and health sciences, symbols.namesake, chemistry.chemical_compound, MESH: Golgi Apparatus, Ribonucleases, MESH: Endoplasmic Reticulum, Genetics, Animals, Humans, Initiation factor, Protein Interaction Domains and Motifs, MESH: Animals, Molecular Biology, MESH: Mice, 030304 developmental biology, Regulation of gene expression, 0303 health sciences, MESH: Protein Interaction Domains and Motifs, MESH: Humans, EIF4G, Endoplasmic reticulum, MESH: Cytoplasm, 030302 biochemistry & molecular biology, EIF4E, Golgi apparatus, MESH: Eukaryotic Initiation Factor-4E, 3. Good health, [SDV] Life Sciences [q-bio], Eukaryotic Initiation Factor-4E, chemistry, MESH: HeLa Cells, symbols, Carrier Proteins, HeLa Cells
Abstract

International audience; The initiation factor 4E (eIF4E) is implicated in most of the crucial steps of the mRNA life cycle and is recognized as a pivotal protein in gene regulation. Many of these roles are mediated by its interaction with specific proteins generally known as eIF4E-interacting partners (4E-IPs), such as eIF4G and 4E-BP. To screen for new 4E-IPs, we developed a novel approach based on structural, in silico and biochemical analyses. We identified the protein Angel1, a member of the CCR4 deadenylase family. Immunoprecipitation experiments provided evidence that Angel1 is able to interact in vitro and in vivo with eIF4E. Point mutation variants of Angel1 demonstrated that the interaction of Angel1 with eIF4E is mediated through a consensus eIF4E-binding motif. Immunofluorescence and cell fractionation experiments showed that Angel1 is confined to the endoplasmic reticulum and Golgi apparatus, where it partially co-localizes with eIF4E and eIF4G, but not with 4E-BP. Furthermore, manipulating Angel1 levels in living cells had no effect on global translation rates, suggesting that the protein has a more specific function. Taken together, our results illustrate that we developed a powerful method for identifying new eIF4E partners and open new perspectives for understanding eIF4E-specific regulation.

Published
2013
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31. mRNA-Selective Translation Induced by FSH in Primary Sertoli Cells

Author

Julia Morales, Nathalie Oulhen, Astrid Musnier, Patrick Vourc'h, Sandrine Boulben, Kelly León, Domitille Heitzler, Eric Reiter, Thomas Boulo, Anne Poupon, Patrick Cormier, Pascale Crépieux, Vlad Costache, Physiologie de la reproduction et des comportements [Nouzilly] (PRC), Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur] (IFCE)-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS), Mer et santé (MS), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Université européenne de Bretagne - European University of Brittany (UEB), Imagerie et cerveau (iBrain - Inserm U1253 - UNIV Tours ), Université de Tours (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de Biochimie et de Biologie Moléculaire, Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), Université de Tours-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre Hospitalier Régional Universitaire de Tours (CHRU TOURS), Centre National de la Recherche Scientifique (CNRS)-Université de Tours-Institut Français du Cheval et de l'Equitation [Saumur]-Institut National de la Recherche Agronomique (INRA), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Imagerie et cerveau, Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS), and Centre Hospitalier Régional Universitaire de Tours (CHRU Tours)

Subjects
Male, Eukaryotic Initiation Factor-4E, 0302 clinical medicine, Endocrinology, Eukaryotic initiation factor, Protein biosynthesis, Phosphorylation, Cells, Cultured, Original Research, 0303 health sciences, TOR Serine-Threonine Kinases, Intracellular Signaling Peptides and Proteins, Ribosomal Protein S6 Kinases, 70-kDa, General Medicine, Sertoli cell, Cell biology, medicine.anatomical_structure, fsh, Receptors, FSH, Signal transduction, Proto-Oncogene Proteins c-fos, RNA Caps, medicine.medical_specialty, sertoli cell, endocrine system, Primary Cell Culture, Biology, 03 medical and health sciences, Internal medicine, Polysome, medicine, Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, RNA, Messenger, Rats, Wistar, Molecular Biology, 030304 developmental biology, Messenger RNA, Sertoli Cells, Phosphoproteins, Rats, réseau de signalisation, Polyribosomes, Protein Biosynthesis, cellule de sertoli, RAT, Follicle Stimulating Hormone, Carrier Proteins, Eukaryotic Initiation Factor-4G, 030217 neurology & neurosurgery
Abstract

FSH is a key hormonal regulator of Sertoli cell secretory activity, required to optimize sperm production. To fulfil its biological function, FSH binds a G protein-coupled receptor, the FSH-R. The FSH-R-transduced signaling network ultimately leads to the transcription or down-regulation of numerous genes. In addition, recent evidence has suggested that FSH might also regulate protein translation. However, this point has never been demonstrated conclusively yet. Here we have addressed this issue in primary rat Sertoli cells endogenously expressing physiological levels of FSH-R. We observed that, within 90 min of stimulation, FSH not only enhanced overall protein synthesis in a mammalian target of rapamycin-dependent manner but also increased the recruitment of mRNA to polysomes. m7GTP pull-down experiments revealed the functional recruitment of mammalian target of rapamycin and p70 S6 kinase to the 5′cap, further supported by the enhanced phosphorylation of one of p70 S6 kinase targets, the eukaryotic initiation factor 4B. Importantly, the scaffolding eukaryotic initiation factor 4G was also recruited, whereas eukaryotic initiation factor 4E-binding protein, the eukaryotic initiation factor 4E generic inhibitor, appeared to play a minor role in translational regulations induced by FSH, in contrast to what is generally observed in response to anabolic factors. This particular regulation of the translational machinery by FSH stimulation might support mRNA-selective translation, as shown here by quantitative RT-PCR amplification of the c-fos and vascular endothelial growth factor mRNA but not of all FSH target mRNA, in polysomal fractions. These findings add a new level of complexity to FSH biological roles in its natural target cells, which has been underappreciated so far.

Published
2012
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32. The translational repressor 4E-BP mediates the hypoxia-induced defects in myotome cells

Author

Ronan Le Bouffant, Valérie Bello, Michèle Beaudry, Nicolas Buisson, Thierry Darribère, Magdalena Hidalgo, Patrick Cormier, Réponses Cellulaires et Fonctionnelles à l'Hypoxie (LRPH), Université Paris 13 (UP13)-Université Sorbonne Paris Cité (USPC)-UFR SMBH, Laboratoire de Biologie du Développement (LBD), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Station biologique de Roscoff [Roscoff] (SBR), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
MESH: Muscle Cells, Embryo, Nonmammalian, [SDV]Life Sciences [q-bio], MESH: Cell Hypoxia, MESH: Anoxia, Xenopus, Muscle Proteins, Apoptosis, Cell Count, Xenopus Proteins, MyoD, Xenopus laevis, 0302 clinical medicine, MESH: Animals, Phosphorylation, Hypoxia, MESH: Xenopus Proteins, 0303 health sciences, EIF4E, MESH: Eukaryotic Initiation Factor-4E, Cell Hypoxia, Cell biology, Somites, MESH: Repressor Proteins, MESH: Protein Biosynthesis, 030220 oncology & carcinogenesis, medicine.symptom, MESH: Oxygen, Protein Binding, Mitosis, Biology, Models, Biological, MESH: Somites, MESH: Muscle Proteins, 03 medical and health sciences, MESH: Xenopus laevis, medicine, Animals, MESH: Protein Binding, Transcription factor, PI3K/AKT/mTOR pathway, 030304 developmental biology, Muscle Cells, MESH: Phosphorylation, MESH: Proto-Oncogene Proteins c-akt, MESH: Cell Count, Cell growth, MESH: Apoptosis, MESH: Models, Biological, MESH: Embryo, Nonmammalian, Cell Biology, MESH: Mitosis, Hypoxia (medical), biology.organism_classification, Molecular biology, Oxygen, Repressor Proteins, Eukaryotic Initiation Factor-4E, Protein Biosynthesis, Proto-Oncogene Proteins c-akt
Abstract

International audience; Cell growth, proliferation, differentiation and survival are influenced by the availability of oxygen. The effect of hypoxia on embryonic cells and the underlying molecular mechanisms to maintain cellular viability are still poorly understood. In this study, we show that hypoxia during Xenopus embryogenesis rapidly leads to a significant developmental delay and to cell apoptosis after prolonged exposure. We provide strong evidence that hypoxia does not affect somitogenesis but affects the number of mitotic cells and muscle-specific protein accumulation in somites, without interfering with the expression of MyoD and MRF4 transcription factors. We also demonstrate that hypoxia reversibly decreases Akt phosphorylation and increases the total amount of the translational repressor 4E-BP, in combination with an increase of the 4E-BP associated with eIF4E. Interestingly, the inhibition of PI3-kinase or mTOR, with LY29002 or rapamycin, respectively, triggers the 4E-BP accumulation in Xenopus embryos. Finally, the overexpression of the non-phosphorylatable 4E-BP protein induces, similar to hypoxia, a decrease in mitotic cells and a decrease in muscle-specific protein accumulation in somites. Taken together, our studies suggest that 4E-BP plays a central role under hypoxia in promoting the cap-independent translation at the expense of cap-dependent translation and triggers specific defects in muscle development.

Published
2012
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33. Dephosphorylation of eIF2α is essential for protein synthesis increase and cell cycle progression after sea urchin fertilization

Author

Stefania Bilotto, Laurent Laguerre, Vlad Costache, Bertrand Cosson, Robert Bellé, Julia Morales, Patrick Cormier, Mer et santé (MS), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Sea urchin, Cell cycle checkpoint, Cell division, Eukaryotic Initiation Factor-2, Biology, Dephosphorylation, 03 medical and health sciences, 0302 clinical medicine, Human fertilization, biology.animal, Protein biosynthesis, Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Phosphorylation, Molecular Biology, 030304 developmental biology, Translation factors, 0303 health sciences, eIF2, Cell Cycle, Cell Biology, Cell biology, Biochemistry, Fertilization, Protein Biosynthesis, Sea Urchins, Protein synthesis, 030217 neurology & neurosurgery, Developmental Biology
Abstract

International audience; The eukaryotic Initiation Factor 2 (eIF2) is a key regulator of protein synthesis in eukaryotic cells, implicated in the initiation step of translation. Fertilization of the sea urchin eggs triggers a rapid increase in protein synthesis activity, which is necessary for the progress into embryonic cell cycles. Here we demonstrate that fertilization triggers eIF2α dephosphorylation, concomitant with an increase in protein synthesis and that induction of the eIF2α phosphorylation is intimately linked with an inhibition of protein synthesis and cell cycle arrest. Using a phospho-mimetic protein microinjected into sea urchin eggs, we showed that dephosphorylation of eIF2α is necessary for protein synthesis activity and cell division progression following fertilization. Our results demonstrate that regulation of eIF2α plays an important role in the protein synthesis rise that occurs during early development following fertilization.

Published
2011
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34. M-phase-specific cdc2 protein kinase phosphorylates the beta subunit of casein kinase II and increases casein kinase II activity

Author

Robert Bellé, Odile Mulner‐Lorillon, Patrick Cormier, Marcel Dorée, Howard Beverley Osborne, Robert Poulhe, and Jean-Claude Labbé

Subjects
Maturation-Promoting Factor, Mitosis, In Vitro Techniques, Mitogen-activated protein kinase kinase, Biochemistry, MAP2K7, Starfish, Xenopus laevis, Adenosine Triphosphate, CDC2 Protein Kinase, Casein kinase 2, alpha 1, Animals, Phosphorylation, MAP kinase kinase kinase, Chemistry, Cell Cycle, Alkaline Phosphatase, Molecular biology, Enzyme Activation, Kinetics, Autoradiography, Electrophoresis, Polyacrylamide Gel, Female, Cyclin-dependent kinase 9, Casein kinase 1, Casein kinase 2, Casein Kinases, Protein Kinases
Abstract

The M-phase-specific cdc2 (cell division control) protein kinase (a component of the M-phase-promoting factor) was found to activate casein kinase II in vitro. The increase in casein kinase II activity ranged over 1.5-5-fold. Increase in activity was prevented if ATP was replaced during the activation reaction by a non-hydrolysable analogue. Alkaline phosphatase treatment of the activated enzyme decreased the activity to the basal level. The beta subunit of casein kinase II was phosphorylated by cdc2 protein kinase at site(s) different from the autophosphorylation sites of the enzyme. Phosphoamino acid analysis showed that the beta subunit was phosphorylated by cdc2 protein kinase at threonine residues while autophosphorylation involved serine residues. Casein kinase II may be part of the cascade which leads to increased phosphorylation of many proteins at M-phase and therefore be involved in the pleiotropic effects of M-phase-promoting factor.

Published
1990
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35. After fertilization of sea urchin eggs, eIF4G is post-translationally modified and associated with the cap-binding protein eIF4E

Author

Julia Morales, Patrick Salaün, Nathalie Oulhen, Bertrand Cosson, Patrick Cormier, Mer et santé (MS), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
MESH: Sequence Homology, Amino Acid, Eukaryotic Initiation Factor-4E, MESH: Amino Acid Sequence, chemistry.chemical_compound, MESH: Protein Structure, Tertiary, 0302 clinical medicine, MESH: Ovum, MESH: Animals, Sphaerechinus granularis, Peptide Chain Initiation, Translational, Sea urchin, Glutathione Transferase, 0303 health sciences, biology, EIF4G, EIF4E, MESH: Eukaryotic Initiation Factor-4G, MESH: Eukaryotic Initiation Factor-4E, Cell biology, 030220 oncology & carcinogenesis, Protein Binding, MESH: Peptide Chain Initiation, Translational, Recombinant Fusion Proteins, Molecular Sequence Data, 03 medical and health sciences, biology.animal, Complementary DNA, MESH: Recombinant Fusion Proteins, Animals, MESH: Protein Binding, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, 030304 developmental biology, Ovum, Messenger RNA, MESH: Glutathione Transferase, Binding Sites, MESH: Molecular Sequence Data, Sequence Homology, Amino Acid, Binding protein, Cell Biology, biology.organism_classification, Molecular biology, MESH: Sea Urchins, Protein Structure, Tertiary, chemistry, MESH: Binding Sites, Fertilization, Sea Urchins, MESH: Fertilization, Eukaryotic Initiation Factor-4G
Abstract

International audience; Release of eukaryotic initiation factor 4E (eIF4E) from its translational repressor eIF4E-binding protein (4E-BP) is a crucial event for the first mitotic division following fertilization of sea urchin eggs. Finding partners of eIF4E following fertilization is crucial to understand how eIF4E functions during this physiological process. The isolation and characterization of cDNA encoding Sphaerechinus granularis eIF4G (SgIF4G) are reported. mRNA of SgIF4G is present as a single 8.5-kb transcript in unfertilized eggs, suggesting that only one ortholog exists in echinoderms. The longest open reading frame predicts a sequence of 5235 nucleotides encoding a deduced polypeptide of 1745 amino acids with a predicted molecular mass of 192 kDa. Among highly conserved domains, SgIF4G protein possesses motifs that correspond to the poly(A) binding protein and eIF4E protein-binding sites. A specific polyclonal antibody was produced and used to characterize the SgIF4G protein in unfertilized and fertilized eggs by SDS-PAGE and western blotting. Multiple differentially migrating bands representing isoforms of sea urchin eIF4G are present in unfertilized eggs. Fertilization triggers modifications of the SgIF4G isoforms and rapid formation of the SgIF4G-eIF4E complex. Whereas rapamycin inhibits the formation of the SgIF4G-eIF4E complex, modification of these SgIF4G isoforms occurs independently from the rapamycin-sensitive pathway. Microinjection of a peptide corresponding to the eIF4E-binding site derived from the sequence of SgIF4G into unfertilized eggs affects the first mitotic division of sea urchin embryos. Association of SgIF4G with eIF4E is a crucial event for the onset of the first mitotic division following fertilization, suggesting that cap-dependent translation is highly regulated during this process. This hypothesis is strengthened by the evidence that microinjection of the cap analog m(7)GDP into unfertilized eggs inhibits the first mitotic division.

Published
2007
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36. The Genome of the Sea Urchin Strongylocentrotus purpuratus

Author

Amro Hamdoun, Virginia Brockton, Huyen Dinh, Qiang Tu, Richard O. Hynes, Maria Ina Arnone, Wratko Hlavina, L. Courtney Smith, Mariano A. Loza, David R. Burgess, Matthew P. Hoffman, Florian Raible, Qiu Autumn Yuan, Geoffrey Okwuonu, Mark Y. Tong, Jennifer Hume, Donna Maglott, Manisha Goel, Olivier Fedrigo, Manuel L. Gonzalez-Garay, Celina E. Juliano, Judith Hernandez, Gary M. Wessel, William F. Marzluff, Audrey J. Majeske, Christian Gache, Louise Duloquin, Xingzhi Song, François Lapraz, Fowler J, Alexandre Souvorov, Jared V. Goldstone, Georgia Panopoulou, Sandra Hines, Kyle M. Judkins, Clay Davis, Christine G. Elsik, Paul Kitts, Mariano Loza-Coll, Greg Wray, Taku Hibino, Eric Röttinger, Allison M. Churcher, Annamaria Locascio, Arcady Mushegian, Masashi Kinukawa, Anna Reade, Katherine M. Buckley, I. R. Gibbons, Bert Gold, Aleksandar Milosavljevic, David Epel, Victor D. Vacquier, Ling Ling Pu, Vincenzo Cavalieri, Erin L. Allgood, Lan Zhang, Lynne V. Nazareth, Constantin N. Flytzanis, Ian Bosdet, Yi-Hsien Su, Zeev Pancer, Matthew L. Rowe, Robert C. Angerer, David R. McClay, William H. Klein, Rachel F. Gray, Julian L. Wong, Shunsuke Yaguchi, Robert Bellé, Aaron J. Mackey, Herath Jayantha Gunaratne, Karl Frederik Bergeron, Bruce P. Brandhorst, Greg Murray, Avis H. Cohen, Stephanie Bell, Kristin Tessmar-Raible, Ian K. Townley, Bertrand Cosson, Thomas D. Glenn, Jongmin Nam, Cynthia A. Bradham, Michael Dean, Joseph Chacko, Anthony J. Robertson, Margherita Branno, Valeria Matranga, K. James Durbin, Esther Miranda, Lili Chen, Eran Elhaik, Robert D. Burke, Rita A. Wright, Paola Oliveri, Sandra L. Lee, Gary W. Moy, Alexander E Primus, Shawn S. McCafferty, Cristina Calestani, David A. Garfield, Erica Sodergren, Karen Wilson, Joel Smith, Marco A. Marra, Cynthia Messier, Julia Morales, Kim D. Pruitt, Rachel Thorn, Rachel Gill, John S. Taylor, Mark E. Hahn, Victor Sapojnikov, Meredith Howard-Ashby, Lynne M. Angerer, Maurice R. Elphick, Kathy R. Foltz, Anne Marie Genevière, Justin T. Reese, Blanca E. Galindo, Kim C. Worley, Andrew Leone, Glen Humphrey, Kevin Berney, Olga Ermolaeva, George Miner, David P. Terwilliger, Elly Suk Hen Chow, Lora Lewis, Dan Graur, C. Titus Brown, Gerard Manning, Kevin J. Peterson, Angela Jolivet, Michele K. Anderson, Francesca Rizzo, Ekaterina Voronina, Thierry Lepage, Giorgio Matassi, Antonio Fernandez-Guerra, Mamoru Nomura, Charles A. Whittaker, James R.R. Whittle, James A. Coffman, George M. Weinstock, Mohammed M. Idris, Ashlan M. Musante, Sebastian D. Fugmann, Katherine D. Walton, Sorin Istrail, Shu-Yu Wu, Cerrissa Hamilton, Jonah Cool, Jacqueline E. Schein, Stacey M. Curry, Athula Wikramanayke, Seth Carbonneau, Blair J. Rossetti, Christopher E. Killian, Melissa J. Landrum, Amanda P. Rawson, Jenifer C. Croce, Ryan C. Range, Rahul Satija, John J. Stegeman, Yufeng Shen, Cavit Agca, Terry Gaasterland, Rocky Cheung, Takae Kiyama, Nikki Adams, Jonathan P. Rast, Robert Piotr Olinski, Andrew Cree, Mark Scally, Shuguang Liang, David A. Parker, Rebecca Thomason, Gretchen E. Hofmann, Michelle M. Roux, Ronghui Xu, Robert A. Obar, Enrique Arboleda, Odile Mulner-Lorillon, Shannon Dugan-Rocha, David J. Bottjer, Gabriele Amore, Manoj P. Samanta, Waraporn Tongprasit, Véronique Duboc, La Ronda Jackson, Fred H. Wilt, Viktor Stolc, Anna T. Neill, Michael Raisch, Pei Yun Lee, Jia L. Song, Margaret Morgan, Brian T. Livingston, Sofia Hussain, Zheng Wei, Bryan J. Cole, Tonya F. Severson, Victor V. Solovyev, Finn Hallböök, Donna M. Muzny, Christine A. Byrum, Albert J. Poustka, Xiuqian Mu, Andrew R. Jackson, Shin Heesun, Euan R. Brown, Nansheng Chen, Patrick Cormier, Ralph Haygood, Pedro Martinez, R. Andrew Cameron, D. Wang, Wendy S. Beane, Eric H. Davidson, Christie Kovar, Hemant Kelkar, Charles A. Ettensohn, Sham V. Nair, Robert L. Morris, Stefan C. Materna, Michael C. Thorndyke, Richard A. Gibbs, Dan O Mellott, Department of Physiology and Biophysics, Stony Brook University [The State University of New York] ( SBU ), Astronomy Unit ( AU ), Queen Mary University of London ( QMUL ), Urban and Industrial Air Quality Group, CSIRO Energy Technology, Commonwealth Scientific and Industrial Research Organisation Energy Technology ( CSIRO Energy Technology ), Commonwealth Scientific and Industrial Research Organisation, Center for Polymer Studies ( CPS ), Boston University [Boston] ( BU ), Physics Department [Boston] ( BU-Physics ), Max Planck Institute for Psycholinguistics, Max-Planck-Institut, Department of Biology [Norton], Wheaton College [Norton], Mathematical Institute [Oxford] ( MI ), University of Oxford [Oxford], Centre for the Analysis of Time Series ( CATS ), London School of Economics and Political Science ( LSE ), Thomas Jefferson National Accelerator Facility ( Jefferson Lab ), Thomas Jefferson National Accelerator Facility, Laboratoire d'Energétique et de Mécanique Théorique Appliquée ( LEMTA ), Université de Lorraine ( UL ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire Evolution, Génomes et Spéciation ( LEGS ), Centre National de la Recherche Scientifique ( CNRS ), Department of Geology, University of Illinois at Urbana-Champaign [Urbana], Department of Electrical and Computer Engineering [Portland] ( ECE ), Portland State University [Portland] ( PSU ), Saint-Gobain Crystals [USA], SAINT-GOBAIN, Institute for Animal Health ( IAH ), Biotechnology and Biological Sciences Research Council, Center for Agricultural Resources Research, Chinese Academy of Sciences [Changchun Branch] ( CAS ), Ipsen Inc. [Milford] ( Ipsen ), IPSEN, Department of Physics [Berkeley], University of California [Berkeley], Institute for Climate and Atmospheric Science [Leeds] ( ICAS ), University of Leeds, Chung-Ang University ( CAU ), Chung-Ang University [Seoul], Antarctic Climate and Ecosystems Cooperative Research Center ( ACE-CRC ), Institute of Aerodynamics and Fluid Mechanics ( AER ), Technische Universität München [München] ( TUM ), Mer et santé ( MS ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Centre National de la Recherche Scientifique ( CNRS ), Imperial College London, Radio and Atmospheric Sciences Division, National Physical Laboratory [Teddington] ( NPL ), International Research Institute for Climate and Society ( IRI ), Earth Institute at Columbia University, Columbia University [New York]-Columbia University [New York], Soils Group, The Macaulay Institute, Department of Haematology, University of Cambridge [UK] ( CAM ), School of Biology and Biochemistry, Queen's University, Leslie Hill Institute for Plant Conservation ( PCU ), University of Cape Town, Institute for Microelectronics and Microsystems/ Istituto per la Microelettronica e Microsistemi ( IMM ), Consiglio Nazionale delle Ricerche ( CNR ), Laboratoire d'acoustique de l'université du Mans ( LAUM ), Le Mans Université ( UM ) -Centre National de la Recherche Scientifique ( CNRS ), Interactive Systems Labs ( ISL ), Carnegie Mellon University [Pittsburgh] ( CMU ), Dalian Institute of Chemical Physics ( DICP ), Architectures, Languages and Compilers to Harness the End of Moore Years ( ALCHEMY ), Laboratoire de Recherche en Informatique ( LRI ), Université Paris-Sud - Paris 11 ( UP11 ) -Institut National de Recherche en Informatique et en Automatique ( Inria ) -CentraleSupélec-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Institut National de Recherche en Informatique et en Automatique ( Inria ) -CentraleSupélec-Centre National de la Recherche Scientifique ( CNRS ) -Inria Saclay - Ile de France, Institut National de Recherche en Informatique et en Automatique ( Inria ), Clean Air Task Force ( CATF ), Clean Air Task Force, Space Physics Laboratory, Indian Space Research Organisation ( ISRO ), Centre d'études et de recherches appliquées à la gestion ( CERAG ), Université Pierre Mendès France - Grenoble 2 ( UPMF ) -Centre National de la Recherche Scientifique ( CNRS ), Department of Microbiology and Immunology, College of Medicine and Health Sciences-Sultan Qaboos University, European Molecular Biology Laboratory [Heidelberg] ( EMBL ), Department of Biostatistics, University of Michigan [Ann Arbor], Department of Radiation Oncology [Michigan] ( Radonc ), Department of Physics and Astronomy [Leicester], University of Leicester, Informatique, Biologie Intégrative et Systèmes Complexes ( IBISC ), Université d'Évry-Val-d'Essonne ( UEVE ) -Centre National de la Recherche Scientifique ( CNRS ), Institut für Meteorologie und Klimaforschung ( IMK ), Karlsruher Institut für Technologie ( KIT ), Physics Department [UNB], University of New Brunswick ( UNB ), Laboratoire Parole et Langage ( LPL ), Centre National de la Recherche Scientifique ( CNRS ) -Aix Marseille Université ( AMU ), Institut des Sciences Chimiques de Rennes ( ISCR ), Université de Rennes 1 ( UR1 ), Université de Rennes ( UNIV-RENNES ) -Université de Rennes ( UNIV-RENNES ) -Ecole Nationale Supérieure de Chimie de Rennes-Institut National des Sciences Appliquées ( INSA ) -Centre National de la Recherche Scientifique ( CNRS ), Biogéosciences [Dijon] ( BGS ), Université de Bourgogne ( UB ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique ( CNRS ), Bioprojet, Laboratoire de Matériaux à Porosité Contrôlée ( LMPC ), Université de Haute-Alsace (UHA) Mulhouse - Colmar ( Université de Haute-Alsace (UHA) ) -Ecole Nationale Supérieure de Chimie de Mulhouse-Centre National de la Recherche Scientifique ( CNRS ), School of Information Engineering [USTB] ( SIE ), University of Science and Technology Beijing [Beijing] ( USTB ), Laboratory for Atmospheric and Space Physics [Boulder] ( LASP ), University of Colorado Boulder [Boulder], Department of Applied Mathematics [Sheffield], University of Sheffield [Sheffield], School of Mathematics and Statistics [Sheffield] ( SoMaS ), Laboratoire de Mécanique de Lille - FRE 3723 ( LML ), Université de Lille, Sciences et Technologies-Ecole Centrale de Lille-Centre National de la Recherche Scientifique ( CNRS ), Computer Science Department [UCLA] ( CSD ), University of California at Los Angeles [Los Angeles] ( UCLA ), Développement et évolution ( DE ), Université Paris-Sud - Paris 11 ( UP11 ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de Biologie du Développement de Villefranche sur mer ( LBDV ), Laboratoire Pierre Aigrain ( LPA ), Fédération de recherche du Département de physique de l'Ecole Normale Supérieure - ENS Paris ( FRDPENS ), Centre National de la Recherche Scientifique ( CNRS ) -École normale supérieure - Paris ( ENS Paris ) -Centre National de la Recherche Scientifique ( CNRS ) -École normale supérieure - Paris ( ENS Paris ) -Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Université Paris Diderot - Paris 7 ( UPD7 ) -Centre National de la Recherche Scientifique ( CNRS ), Department of Mathematics and Statistics [Mac Gill], McGill University, Departamento de Botánica [Comahue], Universidad nacional del Comahue, Bioénergétique Cellulaire et Pathologique ( BECP ), Université Joseph Fourier - Grenoble 1 ( UJF ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ), Environnements et Paléoenvironnements OCéaniques ( EPOC ), Observatoire aquitain des sciences de l'univers ( OASU ), Université Sciences et Technologies - Bordeaux 1-Institut national des sciences de l'Univers ( INSU - CNRS ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Sciences et Technologies - Bordeaux 1-Institut national des sciences de l'Univers ( INSU - CNRS ) -Centre National de la Recherche Scientifique ( CNRS ) -École pratique des hautes études ( EPHE ) -Centre National de la Recherche Scientifique ( CNRS ), Institut Jacques Monod ( IJM ), Université Paris Diderot - Paris 7 ( UPD7 ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratori Nazionali del Sud ( LNS ), National Institute for Nuclear Physics ( INFN ), Departament de Matemàtiques [Barcelona], Universitat Autònoma de Barcelona [Barcelona] ( UAB ), Max-Planck-Institut für Kohlenforschung (coal research), Institute of Oceanology [CAS] ( IOCAS ), National Chiao Tung University ( NCTU ), Department of Hydrology and Water Resources ( HWR ), University of Arizona, Centre for Educational Technology, Environment Department [York], University of York [York, UK], State Key Laboratory of Nuclear Physics and Technology ( SKL-NPT ), Peking University [Beijing], Department of Physics and Astronomy [Iowa City], University of Iowa [Iowa], NASA Ames Research Center ( ARC ), Department of Materials, Digital Language & Knowledge Contents Research Association ( DICORA ), Hankuk University of Foreign Studies, Department of Physics [Coventry], University of Warwick [Coventry], Space Science and Technology Department [Didcot] ( RAL Space ), STFC Rutherford Appleton Laboratory ( RAL ), Science and Technology Facilities Council ( STFC ) -Science and Technology Facilities Council ( STFC ), Institut de biologie et chimie des protéines [Lyon] ( IBCP ), Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique ( CNRS ), H M Nautical Almanac Office [RAL] ( HMNAO ), Rutherford Appleton Laboratory, United Kingdom Met Office [Exeter], University College of London [London] ( UCL ), Department of Pathology and Laboratory Medicine [UCLA], University of California at Los Angeles [Los Angeles] ( UCLA ) -School of Medicine, School of Earth and Environmental Sciences [Seoul] ( SEES ), Seoul National University [Seoul], Department of Chemistry, Seoul Women's University, MicroMachines Centre ( MMC ), Nanyang Technological University [Singapour], Regroupement Québécois sur les Matériaux de Pointe ( RQMP ), École Polytechnique de Montréal ( EPM ) -Université de Sherbrooke [Sherbrooke]-McGill University-Université de Montréal-Fonds Québécois de Recherche sur la Nature et les Technologies ( FQRNT ), Département de Physique [Montréal], Université de Montréal, School of Earth and Environment [Leeds] ( SEE ), Centre for Ecology and Hydrology ( CEH ), Natural Environment Research Council ( NERC ), Norwegian Institute for Water Research ( NIVA ), Norwegian Institute for Water Research, Stony Brook University [SUNY] (SBU), State University of New York (SUNY)-State University of New York (SUNY), Astronomy Unit [London] (AU), Queen Mary University of London (QMUL), Commonwealth Scientific and Industrial Research Organisation Energy Technology (CSIRO Energy Technology), Commonwealth Scientific and Industrial Research Organisation [Canberra] (CSIRO), Department of Biochemistry and Molecular Biology [Houston], The University of Texas Medical School at Houston, Mathematical Institute [Oxford] (MI), University of Oxford, Centre for the Analysis of Time Series (CATS), London School of Economics and Political Science (LSE), Thomas Jefferson National Accelerator Facility (Jefferson Lab), Laboratoire Énergies et Mécanique Théorique et Appliquée (LEMTA ), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Evolution, Génomes et Spéciation (LEGS), Centre National de la Recherche Scientifique (CNRS), University of Illinois System-University of Illinois System, Department of Electrical and Computer Engineering [Portland] (ECE), Portland State University [Portland] (PSU), Saint-Gobain, Institute for Animal Health (IAH), Biotechnology and Biological Sciences Research Council (BBSRC), Chinese Academy of Sciences [Changchun Branch] (CAS), Ipsen Inc. [Milford] (Ipsen), University of California [Berkeley] (UC Berkeley), University of California (UC)-University of California (UC), Institute for Climate and Atmospheric Science [Leeds] (ICAS), School of Earth and Environment [Leeds] (SEE), University of Leeds-University of Leeds, Chung-Ang University (CAU), Antarctic Climate and Ecosystems Cooperative Research Centre (ACE-CRC), Institute of Aerodynamics and Fluid Mechanics (AER), Technische Universität Munchen - Université Technique de Munich [Munich, Allemagne] (TUM), Mer et santé (MS), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), National Physical Laboratory [Teddington] (NPL), International Research Institute for Climate and Society (IRI), Macaulay Institute, University of Cambridge [UK] (CAM), Queen's University [Kingston, Canada], Leslie Hill Institute for Plant Conservation (PCU), Istituto per la Microelettronica e Microsistemi [Catania] (IMM), National Research Council of Italy | Consiglio Nazionale delle Ricerche (CNR), Laboratoire d'Acoustique de l'Université du Mans (LAUM), Le Mans Université (UM)-Centre National de la Recherche Scientifique (CNRS), Interactive Systems Labs (ISL), Carnegie Mellon University [Pittsburgh] (CMU), Dalian Institute of Chemical Physics (DICP), Architectures, Languages and Compilers to Harness the End of Moore Years (ALCHEMY), Laboratoire de Recherche en Informatique (LRI), Université Paris-Sud - Paris 11 (UP11)-CentraleSupélec-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Sud - Paris 11 (UP11)-CentraleSupélec-Centre National de la Recherche Scientifique (CNRS)-Inria Saclay - Ile de France, Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria), Clean Air Task Force (CATF), Indian Space Research Organisation (ISRO), Centre d'études et de recherches appliquées à la gestion (CERAG), Université Pierre Mendès France - Grenoble 2 (UPMF)-Centre National de la Recherche Scientifique (CNRS), Sultan Qaboos University (SQU)-College of Medicine and Health Sciences [Baylor], Baylor University-Baylor University, European Molecular Biology Laboratory [Heidelberg] (EMBL), University of Michigan System-University of Michigan System, Department of Radiation Oncology [Michigan] (Radonc), Informatique, Biologie Intégrative et Systèmes Complexes (IBISC), Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), Institute for Meteorology and Climate Research (IMK), Karlsruhe Institute of Technology (KIT), University of New Brunswick (UNB), Laboratoire Parole et Langage (LPL), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Institut des Sciences Chimiques de Rennes (ISCR), Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Biogéosciences [UMR 6282] (BGS), Université de Bourgogne (UB)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Matériaux à Porosité Contrôlée (LMPC), Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS), School of Information Engineering [USTB] (SIE), University of Science and Technology Beijing [Beijing] (USTB), Laboratory for Atmospheric and Space Physics [Boulder] (LASP), University of Colorado [Boulder], School of Mathematics and Statistics [Sheffield] (SoMaS), Laboratoire de Mécanique de Lille - FRE 3723 (LML), Université de Lille, Sciences et Technologies-Centrale Lille-Centre National de la Recherche Scientifique (CNRS), Computer Science Department [UCLA] (CSD), University of California [Los Angeles] (UCLA), Développement et évolution (DE), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie du Développement de Villefranche sur mer (LBDV), Observatoire océanologique de Villefranche-sur-mer (OOVM), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Pierre Aigrain (LPA), Fédération de recherche du Département de physique de l'Ecole Normale Supérieure - ENS Paris (FRDPENS), École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Department of Mathematics and Statistics [Montréal], McGill University = Université McGill [Montréal, Canada], Departamento de Botánica [Bariloche], Centro Regional Universitario Bariloche [Bariloche] (CRUB), Universidad Nacional del Comahue [Neuquén] (UNCOMA)-Universidad Nacional del Comahue [Neuquén] (UNCOMA), Bioénergétique Cellulaire et Pathologique (BECP), Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Environnements et Paléoenvironnements OCéaniques (EPOC), Observatoire aquitain des sciences de l'univers (OASU), Université Sciences et Technologies - Bordeaux 1 (UB)-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Sciences et Technologies - Bordeaux 1 (UB)-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS)-École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS), Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Laboratori Nazionali del Sud (LNS), Istituto Nazionale di Fisica Nucleare (INFN), Departament de Matemàtiques [Barcelona] (UAB), Universitat Autònoma de Barcelona (UAB), Max-Planck-Institut für Kohlenforschung (Coal Research), Max-Planck-Gesellschaft, CAS Institute of Oceanology (IOCAS), Chinese Academy of Sciences [Beijing] (CAS), National Chiao Tung University (NCTU), Department of Hydrology and Water Resources (HWR), State Key Laboratory of Nuclear Physics and Technology (SKL-NPT), University of Iowa [Iowa City], NASA Ames Research Center (ARC), Digital Language & Knowledge Contents Research Association (DICORA), Space Science and Technology Department [Didcot] (RAL Space), STFC Rutherford Appleton Laboratory (RAL), Science and Technology Facilities Council (STFC)-Science and Technology Facilities Council (STFC), Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), H M Nautical Almanac Office [RAL] (HMNAO), University College of London [London] (UCL), University of California (UC)-University of California (UC)-School of Medicine, School of Earth and Environmental Sciences [Seoul] (SEES), Seoul National University [Seoul] (SNU), MicroMachines Centre (MMC), Regroupement Québécois sur les Matériaux de Pointe (RQMP), École Polytechnique de Montréal (EPM)-Université de Sherbrooke (UdeS)-McGill University = Université McGill [Montréal, Canada]-Université de Montréal (UdeM)-Fonds Québécois de Recherche sur la Nature et les Technologies (FQRNT), Université de Montréal (UdeM), Centre for Ecology and Hydrology (CEH), Natural Environment Research Council (NERC), Norwegian Institute for Water Research (NIVA), SEA URCHIN GENOME SEQUENCING CONSORTIUM, SODERGREN E, WEINSTOCK GM, DAVIDSON EH, CAMERON RA, GIBBS RA, ANGERER RC, ANGERER LM, ARNONE MI, BURGESS DR, BURKE RD, COFFMAN JA, DEAN M, ELPHICK MR, ETTENSOHN CA, FOLTZ KR, HAMDOUN A, HYNES RO, KLEIN WH, MARZLUFF W, MCCLAY DR, MORRIS RL, MUSHEGIAN A, RAST JP, SMITH LC, THORNDYKE MC, VACQUIER VD, WESSEL GM, WRAY G, ZHANG L, ELSIK CG, ERMOLAEVA O, HLAVINA W, HOFMANN G, KITTS P, LANDRUM MJ, MACKEY AJ, MAGLOTT D, PANOPOULOU G, POUSTKA AJ, PRUITT K, SAPOJNIKOV V, SONG X, SOUVOROV A, SOLOVYEV V, WEI Z, WHITTAKER CA, WORLEY K, DURBIN KJ, SHEN Y, FEDRIGO O, GARFIELD D, HAYGOOD R, PRIMUS A, SATIJA R, SEVERSON T, GONZALEZ-GARAY ML, JACKSON AR, MILOSAVLJEVIC A, TONG M, KILLIAN CE, LIVINGSTON BT, WILT FH, ADAMS N, BELLE R, CARBONNEAU S, CHEUNG R, CORMIER P, COSSON B, CROCE J, FERNANDEZ-GUERRA A, GENEVIERE AM, GOEL M, KELKAR H, MORALES J, MULNER-LORILLON O, ROBERTSON AJ, GOLDSTONE JV, COLE B, EPEL D, GOLD B, HAHN ME, HOWARD-ASHBY M, SCALLY M, STEGEMAN JJ, ALLGOOD EL, COOL J, JUDKINS KM, MCCAFFERTY SS, MUSANTE AM, OBAR RA, RAWSON AP, ROSSETTI BJ, GIBBONS IR, HOFFMAN MP, LEONE A, ISTRAIL S, MATERNA SC, SAMANTA MP, STOLC V, TONGPRASIT W, TU Q, BERGERON KF, BRANDHORST BP, WHITTLE J, BERNEY K, BOTTJER DJ, CALESTANI C, PETERSON K, CHOW E, YUAN QA, ELHAIK E, GRAUR D, REESE JT, BOSDET I, HEESUN S, MARRA MA, SCHEIN J, ANDERSON MK, BROCKTON V, BUCKLEY KM, COHEN AH, FUGMANN SD, HIBINO T, LOZA-COLL M, MAJESKE AJ, MESSIER C, NAIR SV, PANCER Z, TERWILLIGER DP, AGCA C, ARBOLEDA E, CHEN N, CHURCHER AM, HALLBOOK F, HUMPHREY GW, IDRIS MM, KIYAMA T, LIANG S, MELLOTT D, MU X, MURRAY G, OLINSKI RP, RAIBLE F, ROWE M, TAYLOR JS, TESSMAR-RAIBLE K, WANG D, WILSON KH, YAGUCHI S, GAASTERLAND T, GALINDO BE, GUNARATNE HJ, JULIANO C, KINUKAWA M, MOY GW, NEILL AT, NOMURA M, RAISCH M, READE A, ROUX MM, SONG JL, SU YH, TOWNLEY IK, VORONINA E, WONG JL, AMORE G, BRANNO M, BROWN ER, CAVALIERI, V, DUBOC V, DULOQUIN L, FLYTZANIS C, GACHE C, LAPRAZ F, LEPAGE T, LOCASCIO A, MART, University of California-University of California, Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), Consiglio Nazionale delle Ricerche (CNR), Centre National de la Recherche Scientifique (CNRS)-Le Mans Université (UM), Centre National de la Recherche Scientifique (CNRS)-Université Pierre Mendès France - Grenoble 2 (UPMF), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Biogéosciences [UMR 6282] [Dijon] (BGS), Centre National de la Recherche Scientifique (CNRS)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Ecole Nationale Supérieure de Chimie de Mulhouse-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences de l'Univers (INSU - CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences de l'Univers (INSU - CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Diderot - Paris 7 (UPD7)-Fédération de recherche du Département de physique de l'Ecole Normale Supérieure - ENS Paris (FRDPENS), Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris), Université Sciences et Technologies - Bordeaux 1-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Sciences et Technologies - Bordeaux 1-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS)-École pratique des hautes études (EPHE), University of California-University of California-School of Medicine, Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS), Université de Lille, Sciences et Technologies-Centre National de la Recherche Scientifique (CNRS)-Centrale Lille, Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF), University of Manchester Institute of Science and Technology (UMIST), Condensed Matter Physics and Materials Science Department, Brookhaven National Laboratory, Brookhaven National Laboratory [Upton, NY] (BNL), UT-Battelle, LLC-Stony Brook University [SUNY] (SBU), State University of New York (SUNY)-State University of New York (SUNY)-U.S. Department of Energy [Washington] (DOE)-UT-Battelle, LLC-Stony Brook University [SUNY] (SBU), State University of New York (SUNY)-State University of New York (SUNY)-U.S. Department of Energy [Washington] (DOE), Baylor College of Medicine (BCM), Baylor University, Laboratoire de Traitement de l'Information Medicale (LaTIM), Université européenne de Bretagne - European University of Brittany (UEB)-Université de Brest (UBO)-Télécom Bretagne-Institut Mines-Télécom [Paris] (IMT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre Hospitalier Régional Universitaire de Brest (CHRU Brest), Laboratoire de Modélisation et Simulation Multi Echelle (MSME), Université Paris-Est Marne-la-Vallée (UPEM)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS), Duke University [Durham], Instituto Andaluz de Geofísica y Prevención de Desastres Sísmicos [Granada] (IAGPDS), Universidad de Granada (UGR), Laboratoire d'Ingénierie des Matériaux de Bretagne (LIMATB), Université de Bretagne Sud (UBS)-Université de Brest (UBO)-Institut Brestois du Numérique et des Mathématiques (IBNM), Université de Brest (UBO)-Université de Brest (UBO), University of New South Wales [Sydney] (UNSW), Celera Genomics (CRA), Celera Genomics, Paléobiodiversité et paléoenvironnements, Muséum national d'Histoire naturelle (MNHN)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Roma Tor Vergata [Roma], Unité de recherches forestières (BORDX PIERR UR ), Institut National de la Recherche Agronomique (INRA), Deptartment of Neuroscience, Uppsala University, State Key Laboratory of Palaeobiology and Stratigraphy, Nanjing Institute of Geology and Palaeontology (NIGPAS-CAS), Chinese Academy of Sciences [Nanjing Branch]-Chinese Academy of Sciences [Nanjing Branch], Institut Méditerranéen d'Ecologie et de Paléoécologie (IMEP), Université Paul Cézanne - Aix-Marseille 3-Université de Provence - Aix-Marseille 1-Avignon Université (AU)-Centre National de la Recherche Scientifique (CNRS), Key Laboratory of Ocean Circulation and Waves, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China, Université Paris Diderot - Paris 7 (UPD7), Department of Physical and Environmental Sciences [Toronto], University of Toronto at Scarborough, inconnu temporaire UPEMLV, Inconnu, Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS), Department of Atmospheric Sciences [Seattle], University of Washington [Seattle], National Institute of Advanced Industrial Science and Technology (AIST), Department of Pharmacy, Università degli studi di Genova = University of Genoa (UniGe), Interdisciplinary Arts and Sciences Department, St. Vincent's Hospital, Sydney, Laboratoire des Sciences de l'Environnement Marin (LEMAR) (LEMAR), Institut de Recherche pour le Développement (IRD)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Université de Brest (UBO)-Institut Universitaire Européen de la Mer (IUEM), Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Department of Electrical Engineering (DEE-POSTECH), Pohang University of Science and Technology (POSTECH), Centre Suisse d'Electronique et de Microtechnique SA [Neuchatel] (CSEM), Centre Suisse d'Electronique et Microtechnique SA (CSEM), Human Genome Sequencing Center [Houston] (HGSC), Brookhaven National Laboratory, Meteorological Service of Canada, 4905 Dufferin Street, Université européenne de Bretagne - European University of Brittany (UEB)-Télécom Bretagne-Centre Hospitalier Régional Universitaire de Brest (CHRU Brest)-Université de Brest (UBO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Mines-Télécom [Paris] (IMT), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Université Paris-Est Marne-la-Vallée (UPEM), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Unité de Recherches Forestières, Department of Physical and Environmental Sciences, University of Toronto [Scarborough, Canada], National Institute for Nuclear Physics (INFN), University of Genoa (UNIGE), Institut de Recherche pour le Développement (IRD)-Institut Universitaire Européen de la Mer (IUEM), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Université de Brest (UBO)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS), Universidad de Granada = University of Granada (UGR), Laboratoire d'Energétique et de Mécanique Théorique Appliquée (LEMTA ), Technische Universität München [München] (TUM), Queen's University [Kingston], Centre National de la Recherche Scientifique (CNRS)-Université Pierre Mendès France - Grenoble 2 (UPMF)-Université Grenoble Alpes (UGA), Institut für Meteorologie und Klimaforschung (IMK), Karlsruher Institut für Technologie (KIT), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Chimie de Rennes-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES), Centre National de la Recherche Scientifique (CNRS)-Université de Lille, Sciences et Technologies-Ecole Centrale de Lille-Université de Lille, Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Université Sciences et Technologies - Bordeaux 1-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Sciences et Technologies - Bordeaux 1-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS)-École pratique des hautes études (EPHE)-Centre National de la Recherche Scientifique (CNRS), Universitat Autònoma de Barcelona [Barcelona] (UAB), École Polytechnique de Montréal (EPM)-Université de Sherbrooke [Sherbrooke]-Université de Montréal [Montréal]-McGill University-Fonds Québécois de Recherche sur la Nature et les Technologies (FQRNT), Université de Montréal [Montréal], U.S. Department of Energy [Washington] (DOE)-UT-Battelle, LLC-Stony Brook University [SUNY] (SBU), Université de Bretagne Sud (UBS)-Institut Brestois du Numérique et des Mathématiques (IBNM), Université de Brest (UBO)-Université de Brest (UBO)-Université de Brest (UBO), Muséum national d'Histoire naturelle (MNHN)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), Université Paul Cézanne - Aix-Marseille 3-Centre National de la Recherche Scientifique (CNRS)-Avignon Université (AU)-Université de Provence - Aix-Marseille 1, Institut Universitaire Européen de la Mer (IUEM), Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Centre National de la Recherche Scientifique (CNRS)-Université de Brest (UBO), Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université de Lille, Sciences et Technologies-Ecole Centrale de Lille-Université de Lille-Centre National de la Recherche Scientifique (CNRS), École normale supérieure - Paris (ENS Paris), and Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Male, MESH: Signal Transduction, MESH: Sequence Analysis, DNA, MESH : Transcription Factors, MESH : Calcification, Physiologic, Genome, MESH : Proteins, 0302 clinical medicine, MESH : Embryonic Development, MESH: Gene Expression Regulation, Developmental, Innate, MESH: Embryonic Development, Developmental, Nervous System Physiological Phenomena, MESH: Animals, MESH: Proteins, [SDV.BDD]Life Sciences [q-bio]/Development Biology, Complement Activation, ComputingMilieux_MISCELLANEOUS, MESH: Evolution, Molecular, MESH : Strongylocentrotus purpuratus, Genetics, 0303 health sciences, MESH: Nervous System Physiological Phenomena, Multidisciplinary, biology, Medicine (all), MESH: Immunologic Factors, Gene Expression Regulation, Developmental, Genome project, MESH: Transcription Factors, MESH : Immunity, Innate, MESH : Complement Activation, MESH: Genes, Bacterial artificial chromosome (BAC)DeuterostomesStrongylocentrotus purpuratusVertebrate innovations, Echinoderm, MESH : Nervous System Physiological Phenomena, embryonic structures, MESH: Cell Adhesion Molecules, MESH : Genes, MESH: Immunity, Innate, Sequence Analysis, Signal Transduction, MESH: Computational Biology, Genome evolution, MESH: Complement Activation, Sequence analysis, Evolution, MESH: Strongylocentrotus purpuratus, MESH : Male, Embryonic Development, MESH : Immunologic Factors, Article, MESH: Calcification, Physiologic, Calcification, MESH : Cell Adhesion Molecules, Evolution, Molecular, 03 medical and health sciences, Calcification, Physiologic, Animals, Immunologic Factors, MESH: Genome, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH : Evolution, Molecular, Physiologic, Gene, Strongylocentrotus purpuratus, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, 030304 developmental biology, MESH : Signal Transduction, Bacterial artificial chromosome, Immunity, Molecular, Computational Biology, Proteins, Cell Adhesion Molecules, Genes, Immunity, Innate, Transcription Factors, Sequence Analysis, DNA, DNA, biology.organism_classification, MESH: Male, Gene Expression Regulation, MESH : Animals, MESH : Gene Expression Regulation, Developmental, MESH : Genome, 030217 neurology & neurosurgery, MESH : Computational Biology, MESH : Sequence Analysis, DNA
Abstract

We report the sequence and analysis of the 814-megabase genome of the sea urchin Strongylocentrotus purpuratus , a model for developmental and systems biology. The sequencing strategy combined whole-genome shotgun and bacterial artificial chromosome (BAC) sequences. This use of BAC clones, aided by a pooling strategy, overcame difficulties associated with high heterozygosity of the genome. The genome encodes about 23,300 genes, including many previously thought to be vertebrate innovations or known only outside the deuterostomes. This echinoderm genome provides an evolutionary outgroup for the chordates and yields insights into the evolution of deuterostomes.

Published
2006
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37. [eIF4E and developmental decisions: when translation drives the development]

Author

Nathalie, Oulhen and Patrick, Cormier

Subjects
Eukaryotic Initiation Factor-4E, Protein Biosynthesis, Animals, Embryonic Development
Abstract

Regulation of mRNA translation is an important regulatory step in gene expression. During embryonic development, mRNA translation is tightly regulated to produce the protein at the right place, at the right time. The eukaryotic initiation factor 4E (eIF4E) is a major target for the regulation of cap-dependent translation, that plays a key role during embryogenesis including gametogenesis, fertilization and establishment of embryonic axes. In this review, we describe recent advances illustrating the importance of the translational regulator eIF4E and its partners in developmental decisions. double dagger.

Published
2006

38. The guanine-nucleotide-exchange complex (EF-1 beta gamma delta) of elongation factor-1 contains two similar leucine-zipper proteins EF-1 delta, p34 encoded by EF-1 delta 1 and p36 encoded by EF-1 delta 2

Author

Odile Mulner-Lorillon, Robert Bellé, Odile Minella, Patrick Cormier, and Robert Poulhe

Subjects
Leucine zipper, DNA, Complementary, Macromolecular Substances, Molecular Sequence Data, Biology, In Vitro Techniques, Biochemistry, HSPA4, Xenopus laevis, Peptide Elongation Factor 1, Complementary DNA, HSPA2, Animals, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, ATF3, Leucine Zippers, HSPA14, Binding Sites, Autophagy-related protein 13, Peptide Elongation Factors, Eukaryotic translation elongation factor 1 alpha 1, Guanine Nucleotides, Molecular Weight, Meiosis, Protein Biosynthesis, Oocytes, Female
Abstract

We have cloned and sequenced a Xenopus cDNA referred to as EF-1 delta 2. The cDNA is homologous to EF-1 delta 1 encoding for EF-1 delta a protein of the guanine-nucleotide exchange complex of elongation factor-1 (EF-1). The protein sequence deduced from the cDNA, contains the two characteristic features of EF-1 delta protein, the leucine-zipper domain and the guanine-nucleotide exchange domain. In vitro and in vivo translation leads to the production of a 36-kDa protein from EF-1 delta and a 34-kDa protein from EF-1 delta 1. The clone EF-1 delta 2 therefore encodes for authentic p36 protein of EF-1 beta gamma delta complex, while EF-1 delta 1 encodes for a newly characterised p34 protein of the leucine zipper family. Both EF-1 delta proteins are simultaneously present in oocytes extracts, at a molecular ratio around 1:10 for p34 versus p36 proteins. Both are associated in a macromolecular structure that is greater than 750 kDa upon gel filtration. The two proteins are targets for Cdc2 kinase in meiotic maturation.

Published
1996

39. Brefeldin A provokes indirect activation of cdc2 kinase (MPF) in Xenopus oocytes, resulting in meiotic cell division

Author

O. Minella, Patrick Cormier, Robert Poulhe, G. Schmalzing, Odile Mulner-Lorillon, Robert Bellé, S. Drewing, ProdInra, Migration, Laboratoire associé de physiologie de la reproduction, Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Recherche Agronomique (INRA), and Institut National de la Recherche Agronomique (INRA)-Université Pierre et Marie Curie - Paris 6 (UPMC)

Subjects
[SDV]Life Sciences [q-bio], Maturation-Promoting Factor, Cyclin B, Xenopus, environment and public health, Xenopus laevis, chemistry.chemical_compound, Oogenesis, Peptide Elongation Factor 1, 0302 clinical medicine, 1-Methyl-3-isobutylxanthine, Cyclic AMP, BIOLOGIE CELLULAIRE, Cycloheximide, Phosphorylation, Progesterone, ComputingMilieux_MISCELLANEOUS, 0303 health sciences, biology, Kinase, Cell Cycle, Cell cycle, Brefeldin A, 3. Good health, Cell biology, [SDV] Life Sciences [q-bio], Meiosis, Mitogen-activated protein kinase, CDC2 Protein Kinase, Signal Transduction, Cholera Toxin, Cyclopentanes, Protamine Kinase, 03 medical and health sciences, Animals, Molecular Biology, 030304 developmental biology, Cyclin-dependent kinase 1, urogenital system, Colforsin, Cell Biology, Peptide Elongation Factors, biology.organism_classification, Enzyme Activation, chemistry, Oocytes, biology.protein, Protein Processing, Post-Translational, 030217 neurology & neurosurgery, Developmental Biology
Abstract

Brefeldin A, a fungal metabolite which disrupts protein traffic, provokes indirect activation of cdc2 protein kinase in Xenopus oocytes. Cdc2 protein kinase activation was judged by MPF (M-phase factor) transfer activity, histone H1 kinase activity, and phosphorylation in vivo of the guanine-nucleotide exchange complex EF-1 beta gamma delta. Oocytes resumed complete meiosis upon brefeldin A treatment. Cdc2 protein kinase, MAP kinase, cyclin B, MPF, and protein synthesis changes were all comparable in brefeldin A-treated oocytes and in progesterone-induced oocytes. ED50 for brefeldin A was 0.6 microM. Brefeldin A activation of cdc2 protein kinase occurs with a long time course. Simultaneous treatment of the oocytes at a subthreshold concentration of 1 nM progesterone and 30 microM brefeldin A considerably shortened the kinetics of maturation. Brefeldin A induction of maturation was sensitive to drugs that act on cAMP metabolism. ID50 for IBMX was 0.1 mM, compared to 1 mM for progesterone-treated oocytes. Brefeldin A inhibited protein traffic in oocytes as determined from protein export experiments. ID50 was between 0.1 and 1 microM. Our results give new insights into the possible mechanism of induction of meiotic maturation and further demonstrate that brefeldin A acts on cell cycle regulatory elements.

Published
1995

40. Elongation factor 1 contains two homologous guanine-nucleotide exchange proteins as shown from the molecular cloning of beta and delta subunits

Author

Robert Bellé, Robert Poulhe, Julia Morales, Odile Mulner-Lorillon, O. Minella, T. Bassez, H. B. Osborne, Patrick Cormier, Université Pierre et Marie Curie - Paris 6 (UPMC), Biologie cellulaire et reproduction, Centre National de la Recherche Scientifique (CNRS), Physiologie de la Reproduction, (UA CNRS 1449 INRA), and Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Guanine, MESH: Peptide Elongation Factors, MESH: Sequence Homology, Amino Acid, Xenopus, Molecular Sequence Data, Restriction Mapping, Sequence Homology, MESH: Amino Acid Sequence, Biology, Molecular cloning, Homology (biology), 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Peptide Elongation Factor 1, Genetics, Animals, Guanine Nucleotide Exchange Factors, MESH: Guanine Nucleotide Exchange Factors, Nucleotide, MESH: Animals, MESH: Xenopus, MESH: Cloning, Molecular, MESH: Proteins, Amino Acid Sequence, MESH: Peptide Elongation Factor 1, Cloning, Molecular, Peptide sequence, MESH: Restriction Mapping, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, MESH: Molecular Sequence Data, Sequence Homology, Amino Acid, Protein primary structure, Molecular, Proteins, Peptide Elongation Factors, Molecular biology, Eukaryotic translation elongation factor 1 alpha 1, Amino Acid, [SDV.BDD.EO]Life Sciences [q-bio]/Development Biology/Embryology and Organogenesis, chemistry, Biochemistry, 030220 oncology & carcinogenesis, Guanine nucleotide exchange factor, Cloning
Abstract

International audience; Elongation factor 1 mediates the elongation step of mRNA translation. The transfer of aminoacyl-tRNA to ribosomes under hydrolysis of GTP is catalyzed by a GTP binding protein, EF1Ia. A guanine-nucleotide exchange complex now referred as EF1beta gamma delta replaces GDP by GTP on EF1alpha (1). A complex, purified from Xenopus oocytes as a substrate for the meiotic and mitotic p34Cdc2 kinase, was shown to contain the guanine-nucleotide exchange activity (2). The Xenopus complex is composed of three main proteins, p30, p36 and p47. Surprisingly, microsequencing of two of its components, p36 and p30 suggested the presence of two related proteins (2). We have previously cloned and sequenced the cDNA encoding for p47 or EF1gamma (3) and p36 or EF1delta (4), we present here the molecular cloning of p30 or EF1beta. This result allows for the first time, sequence analysis of EF1beta and delta proteins, both present in the same complex.

Published
1993

41. Protein phosphatase 2A from Xenopus oocytes. Characterization during meiotic cell division

Author

Thérèse Bassez, Odile Mulner-Lorillon, Robert Poulhe, Patrick Cormier, Robert Bellé, H.Beverley Osborne, Université Pierre et Marie Curie - Paris 6 (UPMC), Biologie cellulaire et reproduction, Centre National de la Recherche Scientifique (CNRS), Physiologie de la Reproduction, (UA CNRS 1449 INRA), and Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Xenopus, Restriction Mapping, MESH: Amino Acid Sequence, MESH: Base Sequence, Biochemistry, 0302 clinical medicine, Structural Biology, Phosphoprotein Phosphatases, MESH: Animals, MESH: Xenopus, Protein Phosphatase 2, Protein phosphatase 2A, MESH: Restriction Mapping, 0303 health sciences, biology, medicine.diagnostic_test, Blotting, MESH: Protein Phosphatase 2, MESH: DNA, 3. Good health, Meiosis, medicine.anatomical_structure, Metaphase-specific form, MESH: Cell Division, Female, Western, Cell Division, MESH: Ovary, Blotting, Western, Molecular Sequence Data, Biophysics, MESH: Oocytes, 03 medical and health sciences, Prophase, Western blot, MESH: Phosphoprotein Phosphatases, MESH: Gene Library, Genetics, medicine, MESH: Blotting, Western, Animals, Amino Acid Sequence, Molecular Biology, Metaphase, 030304 developmental biology, Gene Library, MESH: Molecular Sequence Data, Base Sequence, Ovary, Xenopus meiotic cell division, Cell Biology, Protein phosphatase 2, DNA, Oocyte, biology.organism_classification, Molecular biology, Cytosol, MESH: Meiosis, Associated protein, [SDV.BDD.EO]Life Sciences [q-bio]/Development Biology/Embryology and Organogenesis, Polyclonal antibodies, biology.protein, Oocytes, MESH: Female, 030217 neurology & neurosurgery
Abstract

International audience; A polyclonal antibody was raised against bacterially produced catalytic alpha subunit of protein phosphatase 2A (PP2AC) cloned from Xenopus ovarian library. The amount of PP2AC in Xenopus oocytes determined by Western blot analysis was 1 ng/microgram of cytosolic protein. The antibody depleted PP2AC from oocyte extracts in association with 6 components (40, 62, 65, 80, 85 and 90 kDa). Prophase- and metaphase-arrested oocytes contained identical amounts of PP2AC. Metaphase oocytes showed one specific change in the 62 kDa protein associated with PP2AC.

Published
1991

42. Phosphorylation et synthèse protéique au cours de la méiose de l'ovocyte

Author

O. Mulner-Lorillon, Patrick Cormier, R. Belle, R. Poulhe, and J. Morales

Subjects
Estrous cycle, media_common.quotation_subject, General Medicine, Metabolism, Biology, Oocyte, General Biochemistry, Genetics and Molecular Biology, Cell biology, chemistry.chemical_compound, medicine.anatomical_structure, Meiosis, Biosynthesis, chemistry, medicine, Phosphorylation, Reproduction, media_common
Published
1992
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43. Molecular cloning of a new guaine nucleotide-exchange protein, EF1α

Author

Patrick Cormier, Odile Mulner-Lorillon, Julia Morales, Robert Bellé, and Robert Poulhe

Subjects
Cloning, Genetics, biology, Xenopus, Molecular Sequence Data, Nucleic acid sequence, Molecular cloning, Peptide Elongation Factors, biology.organism_classification, Elongation factor, Peptide Elongation Factor 1, Ribonucleoproteins, Animals, Genomic library, Amino Acid Sequence, Cloning, Molecular, Peptide sequence, Gene Library, Ribonucleoprotein
Published
1992
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44. Molecular cloning ofXenopuselongation factor 1γ, major M-phase promoting factor substrate

Author

Robert Poulhe, Robert Bellé, T. Bassez, Julia Morales, Patrick Cormier, Howard Beverley Osborne, A. Mazabraud, Odile Mulner-Lorillon, Université Pierre et Marie Curie - Paris 6 (UPMC), Biologie cellulaire et reproduction, Centre National de la Recherche Scientifique (CNRS), Centre de génétique moléculaire (CGM), Physiologie de la Reproduction, (UA CNRS 1449 INRA), and Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
MESH: Peptide Elongation Factors, Xenopus, Molecular Sequence Data, Maturation promoting factor, Mitosis, MESH: Amino Acid Sequence, Molecular cloning, Biology, Peptide Elongation Factor 1, Complementary DNA, Genetics, Animals, MESH: Animals, MESH: Cloning, Molecular, MESH: Xenopus, Amino Acid Sequence, MESH: Peptide Elongation Factor 1, Cloning, Molecular, ComputingMilieux_MISCELLANEOUS, MESH: Molecular Sequence Data, Molecular, M-Phase Promoting Factor, MESH: Mitosis, Peptide Elongation Factors, biology.organism_classification, Molecular biology, Eukaryotic translation elongation factor 1 alpha 1, Cell biology, Elongation factor, [SDV.BDD.EO]Life Sciences [q-bio]/Development Biology/Embryology and Organogenesis, biology.protein, Cloning
Abstract

International audience

Published
1991
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45. Cellular coexistence of two high molecular subsets of eEF1B complex

Author

Patrick Cormier, Frédéric Le Sourd, Sandrine Boulben, Odile Mulner-Lorillon, Stéphane Bach, and Robert Bellé

Subjects
Gene isoform, Time Factors, Protein subunit, In silico, Cell, Biophysics, Plasma protein binding, Biology, Biochemistry, Isozyme, Peptide Elongation Factor 1, eEF1B, Structural Biology, Genetics, medicine, Animals, Molecular Biology, chemistry.chemical_classification, Protein translation, Sea urchin egg, Gene Expression Regulation, Developmental, Cell Biology, Molecular biology, Amino acid, Cell biology, Elongation factor, Isoenzymes, Molecular Weight, Protein Subunits, medicine.anatomical_structure, chemistry, Multiprotein Complexes, Sea Urchins, Protein Binding
Abstract

The elongation factor eEF1B involved in protein translation was found to contain two isoforms of the eEF1Bdelta subunit in sea urchin eggs. The eEF1Bdelta2 isoform differs from eEF1Bdelta1 by a specific insert of 26 amino acids. Both isoforms are co-expressed in the cell and likely originate from a unique gene. The feature appears universal in metazoans as judged from in silico analysis in EST-databanks. The eEF1B components were co-immunoprecipitated by specific eEF1Bdelta2 antibodies. Quantification of the proteins in immunoprecipitates and on immunoblots demonstrates that eEF1Bdelta1 and eEF1Bdelta2 proteins are present in two subsets of eEF1B complex. We discuss and propose a model for the different subsets of eEF1B complex concomitantly present in the cell.

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46. Identification of a new isoform of eEF2 whose phosphorylation is required for completion of cell division in sea urchin embryos

Author

Patrick Cormier, Pierre-François Pluchon, Odile Mulner-Lorillon, and Robert Bellé

Subjects
Gene isoform, Cell division, Biology, Cell cycle, EEF2, Dephosphorylation, Peptide Elongation Factor 2, eEF2 isoforms, Protein biosynthesis, Animals, Protein Isoforms, Phosphorylation, Sea urchin embryo, Molecular Biology, Ovum, Protein translation, Cell Biology, Phosphorylated eEF2, Molecular Weight, Elongation factor, Biochemistry, Fertilization, Sea Urchins, Cell Division, Developmental Biology
Abstract

Elongation factor 2 (eEF2) is the main regulator of peptide chain elongation in eukaryotic cells. Using sea urchin eggs and early embryos, two isoforms of eEF2 of respectively 80 and 83kDa apparent molecular weight have been discovered. Both isoforms were identified by immunological analysis as well as mass spectrometry, and appeared to originate from a unique post-translationally modified protein. Accompanying the net increase in protein synthesis that occurs in early development, both eEF2 isoforms underwent dephosphorylation in the 15min period following fertilization, in accordance with the active role of dephosphorylated eEF2 in regulation of protein synthesis. After initial dephosphorylation, the major 83kDa isoform remained dephosphorylated while the 80kDa isoform was progressively re-phosphorylated in a cell-cycle dependent fashion. In vivo inhibition of phosphorylation of the 80kDa isoform impaired the completion of the first cell cycle of early development implicating the involvement of eEF2 phosphorylation in the exit from mitosis.

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47. Purification of a p47 phosphoprotein from Xenopus laevis oocytes and identification as an in vivo and in vitro p34cdc2 substrate

Author

Patrick Cormier, Odile Mulner-Lorillon, Robert Bellé, Robert Poulhe, Marcel Dorée, and Jean-Claude Labbé

Subjects
inorganic chemicals, Cell division, Maturation-Promoting Factor, Biophysics, Xenopus, Biology, Biochemistry, Protamine kinase, Xenopus laevis, Adenosine Triphosphate, Structural Biology, In vivo, CDC2 Protein Kinase, Genetics, Cyclic AMP, Animals, Chymotrypsin, Phosphorylation, Growth Substances, Molecular Biology, Molecular mass, Kinase, Serine Endopeptidases, Cell Biology, Protamine Kinase, biology.organism_classification, Phosphoproteins, In vitro, Peptide Fragments, Cell biology, Molecular Weight, Meiosis, Phosphoprotein, Oocytes, Electrophoresis, Polyacrylamide Gel, Female, Promoting factor, M-phase, Casein Kinases, Protein Kinases
Abstract

This paper describes the purification of a 47 kDa protein from Xenopus laevis oocytes that becomes phosphorylated when the oocytes undergo meiotic maturation. This protein (p47) is part of a high molecular mass complex containing at least two other proteins of molecular mass 30 and 36 kDa. This complex can be isolated from stage VI oocytes before maturation. We obtained a pattern for phosphopeptides in p47 phosphorylated in vivo very similar to that of the purified protein phosphorylated in vitro by p34cdc2 (a H1 kinase which is a component of the M-phase promoting factor) and [γ-32P]ATP. Therefore, the purified p47, already described as a marker of MPF activity, is the first reported in vivo substrate for the cell division control kinase.

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48. Involvement of protein kinase A and casein kinase II in the in vivo protein kinase activities in prophase arrested Xenopus oocytes

Author

Odile Mulner-Lorillon, Patrick Cormier, Robert Bellé, and René Ozon

Subjects
Biophysics, Mitogen-activated protein kinase kinase, Biochemistry, Prophase, Substrate Specificity, Xenopus laevis, Casein kinase 2, alpha 1, Animals, Phosphorylation, Molecular Biology, biology, MAP kinase kinase kinase, Cyclin-dependent kinase 4, Chemistry, Cyclin-dependent kinase 2, Caseins, Cell Biology, Molecular biology, biology.protein, Oocytes, Cyclin-dependent kinase 9, Female, Casein kinase 1, Casein kinase 2, Casein Kinases, Protein Kinases
Abstract

In vivo β casein phosphorylation was analysed in Xenopus full-grown oocytes arrested in the prophase of the meiotic cell division. The phosphorylation was inhibited by the protein kinase inhibitor (PKI) and also by heparin (3 μg/ml; final concentration). β casein phosphorylation was increased by spermine (2 mM). Therefore, protein kinase A and casein kinase II are both active in vivo in full-grown oocytes and may be involved in the prophase arrest of meiotic cell division.

Published
1989

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