17 results on '"Delphin C"'
Search Results
2. Modeling disease-correlated TUBA1A mutation in budding yeast reveals a molecular basis for tubulin dysfunction
- Author
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Denarier, E., primary, Ecklund, K.H., additional, Berthier, G., additional, Favier, A., additional, Gory, S., additional, Macedo, L. De, additional, Delphin, C., additional, Andrieux, A., additional, Markus, S.M., additional, and Boscheron, C., additional
- Published
- 2020
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3. RECOGNITION OF FONT AND TAMIL LETTER IN IMAGES USING DEEP LEARNING
- Author
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Manikandan SRIDHARAN, Delphin Carolina RANI ARULANANDAM, Rajeswari K CHINNASAMY, Suma THIMMANNA, and Sivabalaselvamani DHANDAPANI
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deep convolution network ,tamil letter ,recognition system ,font recognition ,filtering ,Information technology ,T58.5-58.64 ,Electronic computers. Computer science ,QA75.5-76.95 - Abstract
This paper proposes a deep learning approach to recognize Tamil Letter from images which contains text. This is recognition process, the text in the images are divided to letter or characters. Each recognized letters are sending to recognition system and filter the text using deep learning algorithms. Our proposed algorithm is used to separate letter from the text using convolution neural network approach. The filtering system is used for identifying font based on that letters are found. The Tamil letters are test data and loaded in recognition systems. The trained data are input which contains filtered letter from image. For example, Tamil letters such as are available in test dataset. The trained data are applied into deep convolution neural network process. The two dataset are created which contains test data with Tamil letter and second one for recognized input data or trained data. 15 thousands of letters are taken and 512 X 512 X 3 size deep convolution network is created with font and letters. As the result, 85% Tamil letters are recognized and 82% are tested using font. TensorFlow is used for testing the accuracy and success rate.
- Published
- 2021
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4. Validity and Test-Retest Reliability of Spatiotemporal Running Parameter Measurement Using Embedded Inertial Measurement Unit Insoles.
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Riglet L, Orliac B, Delphin C, Leonard A, Eby N, Ornetti P, Laroche D, and Gueugnon M
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- Humans, Male, Adult, Female, Reproducibility of Results, Biomechanical Phenomena physiology, Gait Analysis methods, Shoes, Young Adult, Running physiology, Gait physiology
- Abstract
Running is the basis of many sports and has highly beneficial effects on health. To increase the understanding of running, DSPro
® insoles were developed to collect running parameters during tasks. However, no validation has been carried out for running gait analysis. The aims of this study were to assess the test-retest reliability and criterion validity of running gait parameters from DSPro® insoles compared to a motion-capture system. Equipped with DSPro® insoles, a running gait analysis was performed on 30 healthy participants during overground and treadmill running using a motion-capture system. Using an intraclass correlation coefficient (ICC), the criterion validity and test-retest reliability of spatiotemporal parameters were calculated. The test-retest reliability shows moderate to excellent ICC values (ICC > 0.50) except for propulsion time during overground running at a fast speed with the motion-capture system. The criterion validity highlights a validation of running parameters regardless of speeds (ICC > 0.70). This present study validates the good criterion validity and test-retest reliability of DSPro® insoles for measuring spatiotemporal running gait parameters. Without the constraints of a 3D motion-capture system, such insoles seem to be helpful and relevant for improving the care management of active patients or following running performance in sports contexts.- Published
- 2024
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5. Stable GDP-tubulin islands rescue dynamic microtubules.
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Bagdadi N, Wu J, Delaroche J, Serre L, Delphin C, De Andrade M, Carcel M, Nawabi H, Pinson B, Vérin C, Couté Y, Gory-Fauré S, Andrieux A, Stoppin-Mellet V, and Arnal I
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- Animals, Guanosine Triphosphate metabolism, Humans, Microtubules metabolism, Tubulin metabolism, Tubulin genetics, Guanosine Diphosphate metabolism
- Abstract
Microtubules are dynamic polymers that interconvert between phases of growth and shrinkage, yet they provide structural stability to cells. Growth involves hydrolysis of GTP-tubulin to GDP-tubulin, which releases energy that is stored within the microtubule lattice and destabilizes it; a GTP cap at microtubule ends is thought to prevent GDP subunits from rapidly dissociating and causing catastrophe. Here, using in vitro reconstitution assays, we show that GDP-tubulin, usually considered inactive, can itself assemble into microtubules, preferentially at the minus end, and promote persistent growth. GDP-tubulin-assembled microtubules are highly stable, displaying no detectable spontaneous shrinkage. Strikingly, islands of GDP-tubulin within dynamic microtubules stop shrinkage events and promote rescues. Microtubules thus possess an intrinsic capacity for stability, independent of accessory proteins. This finding provides novel mechanisms to explain microtubule dynamics., (© 2024 Bagdadi et al.)
- Published
- 2024
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6. 3D motion analysis dataset of healthy young adult volunteers walking and running on overground and treadmill.
- Author
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Riglet L, Delphin C, Claquesin L, Orliac B, Ornetti P, Laroche D, and Gueugnon M
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- Humans, Young Adult, Biomechanical Phenomena, Healthy Volunteers, Adult, Gait Analysis, Male, Exercise Test, Walking, Running physiology, Gait
- Abstract
Used on clinical and sportive context, three-dimensional motion analysis is considered as the gold standard in the biomechanics field. The proposed dataset has been established on 30 asymptomatic young participants. Volunteers were asked to walk at slow, comfortable and fast speeds, and to run at comfortable and fast speeds on overground and treadmill using shoes. Three dimensional trajectories of 63 reflective markers, 3D ground reaction forces and moments were simultaneously recorded. A total of 4840 and 18159 gait cycles were measured for overground and treadmill walking, respectively. Additionally, 2931 and 18945 cycles were measured for overground and treadmill running, respectively. The dataset is presented in C3D and CSV files either in raw or pre-processed format. The aim of this dataset is to provide a complete set of data that will help for the gait characterization during clinical gait analysis and in a sportive context. This data could be used for the creation of a baseline database for clinical purposes to research activities exploring the gait and the run., (© 2024. The Author(s).)
- Published
- 2024
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7. IMPROVE study protocol, investigating post-stroke local muscle vibrations to promote cerebral plasticity and functional recovery: a single-blind randomised controlled trial.
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Julliand S, Papaxanthis C, Delphin C, Mock A, Raumel MA, Gueugnon M, Ornetti P, and Laroche D
- Subjects
- Humans, Adolescent, Vibration therapeutic use, Single-Blind Method, Treatment Outcome, Upper Extremity, Muscle Spasticity etiology, Muscles, Randomized Controlled Trials as Topic, Stroke Rehabilitation methods, Stroke therapy
- Abstract
Introduction: Spasticity is a frequent disabling consequence following a stroke. Local muscle vibrations (LMVs) have been proposed as a treatment to address this problem. However, little is known about their clinical and neurophysiological impacts when used repeatedly during the subacute phase post-stroke. This project aims to evaluate the effects of a 6-week LMV protocol on the paretic limb on spasticity development in a post-stroke subacute population., Methods and Analysis: This is an interventional, controlled, randomised, single-blind (patient) trial. 100 participants over 18 years old will be recruited, within 6 weeks following a first stroke with hemiparesis or hemiplegia. All participants will receive a conventional rehabilitation programme, plus 18 sessions of LMV (ie, continuously for 30 min) on relaxed wrist and elbow flexors: either (1) at 80 Hz for the interventional group or (2) at 40 Hz plus a foam band between the skin and the device for the control group.Participants will be evaluated at baseline, at 3 weeks and 6 weeks, and at 6 months after the end of the intervention. Spasticity will be measured by the modified Ashworth scale and with an isokinetic dynamometer. Sensorimotor function will be assessed with the Fugl-Meyer assessment of the upper extremity. Corticospinal and spinal excitabilities will be measured each time., Ethics and Dissemination: This study was recorded in a clinical trial and obtained approval from the institutional review board (Comité de protection des personnes Ile de France IV, 2021-A03219-32). All participants will be required to provide informed consent. The results of this trial will be published in peer-reviewed journals to disseminate information to clinicians and impact their practice for an improved patient's care., Trial Registration Number: Clinical Trial: NCT05315726 DATASET: EUDRAct., Competing Interests: Competing interests: None declared., (© Author(s) (or their employer(s)) 2024. Re-use permitted under CC BY-NC. No commercial re-use. See rights and permissions. Published by BMJ.)
- Published
- 2024
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8. Cryo-EM Visualization of Neuronal Particles Inside Microtubules.
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Gory-Fauré S, Delaroche J, Cuveillier C, Delphin C, and Arnal I
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- Animals, Cryoelectron Microscopy methods, Hippocampus, Mice, Microtubules metabolism, Neurons
- Abstract
Neuronal microtubules have long been known to contain intraluminal particles, called MIPs (microtubule inner proteins), most likely involved in the extreme stability of microtubules in neurons. This chapter describes a cryo-electron microscopy-based assay to visualize microtubules containing neuronal MIPs. We present two protocols to prepare MIPs-containing microtubules, using either in vitro microtubule polymerization assays or extraction of microtubules from mouse hippocampal neurons in culture., (© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)
- Published
- 2022
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9. CRMP4-mediated fornix development involves Semaphorin-3E signaling pathway.
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Boulan B, Ravanello C, Peyrel A, Bosc C, Delphin C, Appaix F, Denarier E, Kraut A, Jacquier-Sarlin M, Fournier A, Andrieux A, Gory-Fauré S, and Deloulme JC
- Subjects
- Animals, Female, Fornix, Brain metabolism, Male, Mice, Nerve Tissue Proteins metabolism, Semaphorins metabolism, Fornix, Brain growth & development, Nerve Tissue Proteins genetics, Semaphorins genetics, Signal Transduction
- Abstract
Neurodevelopmental axonal pathfinding plays a central role in correct brain wiring and subsequent cognitive abilities. Within the growth cone, various intracellular effectors transduce axonal guidance signals by remodeling the cytoskeleton. Semaphorin-3E (Sema3E) is a guidance cue implicated in development of the fornix, a neuronal tract connecting the hippocampus to the hypothalamus. Microtubule-associated protein 6 (MAP6) has been shown to be involved in the Sema3E growth-promoting signaling pathway. In this study, we identified the collapsin response mediator protein 4 (CRMP4) as a MAP6 partner and a crucial effector in Sema3E growth-promoting activity. CRMP4-KO mice displayed abnormal fornix development reminiscent of that observed in Sema3E-KO mice. CRMP4 was shown to interact with the Sema3E tripartite receptor complex within detergent- resistant membrane (DRM) domains, and DRM domain integrity was required to transduce Sema3E signaling through the Akt/GSK3 pathway. Finally, we showed that the cytoskeleton-binding domain of CRMP4 is required for Sema3E's growth-promoting activity, suggesting that CRMP4 plays a role at the interface between Sema3E receptors, located in DRM domains, and the cytoskeleton network. As the fornix is affected in many psychiatric diseases, such as schizophrenia, our results provide new insights to better understand the neurodevelopmental components of these diseases., Competing Interests: BB, CR, AP, CB, CD, FA, ED, AK, MJ, AF, AA, SG, JD No competing interests declared, (© 2021, Boulan et al.)
- Published
- 2021
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10. Beyond Neuronal Microtubule Stabilization: MAP6 and CRMPS, Two Converging Stories.
- Author
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Cuveillier C, Boulan B, Ravanello C, Denarier E, Deloulme JC, Gory-Fauré S, Delphin C, Bosc C, Arnal I, and Andrieux A
- Abstract
The development and function of the central nervous system rely on the microtubule (MT) and actin cytoskeletons and their respective effectors. Although the structural role of the cytoskeleton has long been acknowledged in neuronal morphology and activity, it was recently recognized to play the role of a signaling platform. Following this recognition, research into Microtubule Associated Proteins (MAPs) diversified. Indeed, historically, structural MAPs-including MAP1B, MAP2, Tau, and MAP6 (also known as STOP);-were identified and described as MT-binding and -stabilizing proteins. Extensive data obtained over the last 20 years indicated that these structural MAPs could also contribute to a variety of other molecular roles. Among multi-role MAPs, MAP6 provides a striking example illustrating the diverse molecular and cellular properties of MAPs and showing how their functional versatility contributes to the central nervous system. In this review, in addition to MAP6's effect on microtubules, we describe its impact on the actin cytoskeleton, on neuroreceptor homeostasis, and its involvement in signaling pathways governing neuron development and maturation. We also discuss its roles in synaptic plasticity, brain connectivity, and cognitive abilities, as well as the potential relationships between the integrated brain functions of MAP6 and its molecular activities. In parallel, the Collapsin Response Mediator Proteins (CRMPs) are presented as examples of how other proteins, not initially identified as MAPs, fall into the broader MAP family. These proteins bind MTs as well as exhibiting molecular and cellular properties very similar to MAP6. Finally, we briefly summarize the multiple similarities between other classical structural MAPs and MAP6 or CRMPs.In summary, this review revisits the molecular properties and the cellular and neuronal roles of the classical MAPs, broadening our definition of what constitutes a MAP., Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (Copyright © 2021 Cuveillier, Boulan, Ravanello, Denarier, Deloulme, Gory-Fauré, Delphin, Bosc, Arnal and Andrieux.)
- Published
- 2021
- Full Text
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11. Imaging Microtubules in vitro at High Resolution while Preserving their Structure.
- Author
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Cuveillier C, Saoudi Y, Arnal I, and Delphin C
- Abstract
Microtubules (MT) are the most rigid component of the cytoskeleton. Nevertheless, they often appear highly curved in the cellular context and the mechanisms governing their overall shape are poorly understood. Currently, in vitro microtubule analysis relies primarily on electron microscopy for its high resolution and Total Internal Reflection Fluorescence (TIRF) microscopy for its ability to image live fluorescently-labelled microtubules and associated proteins. For three-dimensional analyses of microtubules with micrometer curvatures, we have developed an assay in which MTs are polymerized in vitro from MT seeds adhered to a glass slide in a manner similar to conventional TIRF microscopy protocols. Free fluorescent molecules are removed and the MTs are fixed by perfusion. The MTs can then be observed using a confocal microscope with an Airyscan module for higher resolution. This protocol allows the imaging of microtubules that have retained their original three-dimensional shape and is compatible with high-resolution immunofluorescence detection., Competing Interests: Competing interestsThe authors declare no competing interests., (Copyright © 2021 The Authors; exclusive licensee Bio-protocol LLC.)
- Published
- 2021
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12. MAP6 is an intraluminal protein that induces neuronal microtubules to coil.
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Cuveillier C, Delaroche J, Seggio M, Gory-Fauré S, Bosc C, Denarier E, Bacia M, Schoehn G, Mohrbach H, Kulić I, Andrieux A, Arnal I, and Delphin C
- Subjects
- Animals, Mice, Microtubules metabolism, Models, Biological, Neurites, Neurons ultrastructure, Protein Binding, Protein Transport, Microtubule-Associated Proteins metabolism, Neurons metabolism
- Abstract
Neuronal activities depend heavily on microtubules, which shape neuronal processes and transport myriad molecules within them. Although constantly remodeled through growth and shrinkage events, neuronal microtubules must be sufficiently stable to maintain nervous system wiring. This stability is somehow maintained by various microtubule-associated proteins (MAPs), but little is known about how these proteins work. Here, we show that MAP6, previously known to confer cold stability to microtubules, promotes growth. More unexpectedly, MAP6 localizes in the lumen of microtubules, induces the microtubules to coil into a left-handed helix, and forms apertures in the lattice, likely to relieve mechanical stress. These features have not been seen in microtubules before and could play roles in maintaining axonal width or providing flexibility in the face of compressive forces during development., (Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).)
- Published
- 2020
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13. Calcium influx mediates the chemoattractant-induced translocation of the arrestin-related protein AdcC in Dictyostelium .
- Author
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Mas L, Cieren A, Delphin C, Journet A, and Aubry L
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- Amino Acid Sequence, Animals, Arrestins chemistry, Cell Membrane drug effects, Cell Membrane metabolism, Cyclic AMP pharmacology, Dictyostelium drug effects, Folic Acid pharmacology, Green Fluorescent Proteins metabolism, Intracellular Space metabolism, Liposomes, Phospholipids metabolism, Protein Binding drug effects, Protein Domains, Protein Multimerization, Protein Transport drug effects, Protozoan Proteins chemistry, Recombinant Proteins metabolism, Arrestins metabolism, Calcium metabolism, Chemotactic Factors pharmacology, Dictyostelium metabolism, Protozoan Proteins metabolism
- Abstract
Arrestins are key adaptor proteins that control the fate of cell-surface membrane proteins and modulate downstream signaling cascades. The Dictyostelium discoideum genome encodes six arrestin-related proteins, harboring additional modules besides the arrestin domain. Here, we studied AdcB and AdcC, two homologs that contain C2 and SAM domains. We showed that AdcC - in contrast to AdcB - responds to various stimuli (such as the chemoattractants cAMP and folate) known to induce an increase in cytosolic calcium by transiently translocating to the plasma membrane, and that calcium is a direct regulator of AdcC localization. This response requires the calcium-dependent membrane-targeting C2 domain and the double SAM domain involved in AdcC oligomerization, revealing a mode of membrane targeting and regulation unique among members of the arrestin clan. AdcB shares several biochemical properties with AdcC, including in vitro binding to anionic lipids in a calcium-dependent manner and auto-assembly as large homo-oligomers. AdcB can interact with AdcC; however, its intracellular localization is insensitive to calcium. Therefore, despite their high degree of homology and common characteristics, AdcB and AdcC are likely to fulfill distinct functions in amoebae., Competing Interests: Competing interestsThe authors declare no competing or financial interests., (© 2018. Published by The Company of Biologists Ltd.)
- Published
- 2018
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14. A key function for microtubule-associated-protein 6 in activity-dependent stabilisation of actin filaments in dendritic spines.
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Peris L, Bisbal M, Martinez-Hernandez J, Saoudi Y, Jonckheere J, Rolland M, Sebastien M, Brocard J, Denarier E, Bosc C, Guerin C, Gory-Fauré S, Deloulme JC, Lanté F, Arnal I, Buisson A, Goldberg Y, Blanchoin L, Delphin C, and Andrieux A
- Subjects
- Animals, Calcium-Calmodulin-Dependent Protein Kinase Type 2 metabolism, Cells, Cultured, Fluorescence Resonance Energy Transfer, Hippocampus cytology, Humans, Mice, Inbred C57BL, Mice, Knockout, Mice, Transgenic, Microtubule-Associated Proteins genetics, Microtubules metabolism, Neurons metabolism, Phosphorylation, Photobleaching, Actin Cytoskeleton metabolism, Dendrites metabolism, Microtubule-Associated Proteins metabolism, Neurons cytology
- Abstract
Emerging evidence indicates that microtubule-associated proteins (MAPs) are implicated in synaptic function; in particular, mice deficient for MAP6 exhibit striking deficits in plasticity and cognition. How MAP6 connects to plasticity mechanisms is unclear. Here, we address the possible role of this protein in dendritic spines. We find that in MAP6-deficient cortical and hippocampal neurons, maintenance of mature spines is impaired, and can be restored by expressing a stretch of the MAP6 sequence called Mc modules. Mc modules directly bind actin filaments and mediate activity-dependent stabilisation of F-actin in dendritic spines, a key event of synaptic plasticity. In vitro, Mc modules enhance actin filament nucleation and promote the formation of stable, highly ordered filament bundles. Activity-induced phosphorylation of MAP6 likely controls its transfer to the spine cytoskeleton. These results provide a molecular explanation for the role of MAP6 in cognition, enlightening the connection between cytoskeletal dysfunction, synaptic impairment and neuropsychiatric illnesses.
- Published
- 2018
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15. Motor axon navigation relies on Fidgetin-like 1-driven microtubule plus end dynamics.
- Author
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Fassier C, Fréal A, Gasmi L, Delphin C, Ten Martin D, De Gois S, Tambalo M, Bosc C, Mailly P, Revenu C, Peris L, Bolte S, Schneider-Maunoury S, Houart C, Nothias F, Larcher JC, Andrieux A, and Hazan J
- Subjects
- Adenosine Triphosphatases chemistry, Animals, Cytoskeleton metabolism, Gene Knockdown Techniques, Growth Cones metabolism, Humans, Larva metabolism, Locomotion, Microtubule-Associated Proteins metabolism, Motor Neurons metabolism, Nuclear Proteins chemistry, Polymerization, Protein Isoforms metabolism, Spinal Cord metabolism, Adenosine Triphosphatases metabolism, Axon Guidance, Axons metabolism, Microtubules metabolism, Nuclear Proteins metabolism
- Abstract
During neural circuit assembly, extrinsic signals are integrated into changes in growth cone (GC) cytoskeleton underlying axon guidance decisions. Microtubules (MTs) were shown to play an instructive role in GC steering. However, the numerous actors required for MT remodeling during axon navigation and their precise mode of action are far from being deciphered. Using loss- and gain-of-function analyses during zebrafish development, we identify in this study the meiotic clade adenosine triphosphatase Fidgetin-like 1 (Fignl1) as a key GC-enriched MT-interacting protein in motor circuit wiring and larval locomotion. We show that Fignl1 controls GC morphology and behavior at intermediate targets by regulating MT plus end dynamics and growth directionality. We further reveal that alternative translation of Fignl1 transcript is a sophisticated mechanism modulating MT dynamics: a full-length isoform regulates MT plus end-tracking protein binding at plus ends, whereas shorter isoforms promote their depolymerization beneath the cell cortex. Our study thus pinpoints Fignl1 as a multifaceted key player in MT remodeling underlying motor circuit connectivity., (© 2018 Fassier et al.)
- Published
- 2018
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16. Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation.
- Author
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Aillaud C, Bosc C, Peris L, Bosson A, Heemeryck P, Van Dijk J, Le Friec J, Boulan B, Vossier F, Sanman LE, Syed S, Amara N, Couté Y, Lafanechère L, Denarier E, Delphin C, Pelletier L, Humbert S, Bogyo M, Andrieux A, Rogowski K, and Moutin MJ
- Subjects
- Angiogenic Proteins genetics, Animals, Carboxypeptidases genetics, Carrier Proteins genetics, Cell Cycle Proteins genetics, Cell Movement, Female, Gene Knockdown Techniques, HEK293 Cells, Humans, Male, Mice, Neocortex cytology, Neocortex embryology, Neurons enzymology, Proteomics, Tubulin metabolism, Angiogenic Proteins metabolism, Carboxypeptidases metabolism, Carrier Proteins metabolism, Cell Cycle Proteins metabolism, Neurogenesis, Neurons cytology, Tyrosine metabolism
- Abstract
Reversible detyrosination of α-tubulin is crucial to microtubule dynamics and functions, and defects have been implicated in cancer, brain disorganization, and cardiomyopathies. The identity of the tubulin tyrosine carboxypeptidase (TCP) responsible for detyrosination has remained unclear. We used chemical proteomics with a potent irreversible inhibitor to show that the major brain TCP is a complex of vasohibin-1 (VASH1) with the small vasohibin binding protein (SVBP). VASH1 and its homolog VASH2, when complexed with SVBP, exhibited robust and specific Tyr/Phe carboxypeptidase activity on microtubules. Knockdown of vasohibins or SVBP and/or inhibitor addition in cultured neurons reduced detyrosinated α-tubulin levels and caused severe differentiation defects. Furthermore, knockdown of vasohibins disrupted neuronal migration in developing mouse neocortex. Thus, vasohibin/SVBP complexes represent long-sought TCP enzymes., (Copyright © 2017 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.)
- Published
- 2017
- Full Text
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17. Refilins are short-lived Actin-bundling proteins that regulate lamellipodium protrusion dynamics.
- Author
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Gay O, Gilquin B, Assard N, Stuelsatz P, Delphin C, Lachuer J, Gidrol X, and Baudier J
- Abstract
Refilins (RefilinA and RefilinB) are members of a novel family of Filamin binding proteins that function as molecular switches to conformationally alter the Actin filament network into bundles. We show here that Refilins are extremely labile proteins. An N-terminal PEST/DSG(X)
2-4 S motif mediates ubiquitin-independent rapid degradation. A second degradation signal is localized within the C-terminus. Only RefilinB is protected from rapid degradation by an auto-inhibitory domain that masks the PEST/DSG(X)2-4 S motif. Dual regulation of RefilinA and RefilinB stability was confirmed in rat brain NG2 precursor cells (polydendrocyte). Using loss- and gain-of-function approaches we show that in these cells, and in U373MG cells, Refilins contribute to the dynamics of lamellipodium protrusion by catalysing Actin bundle formation within the lamella Actin network. These studies extend the Actin bundling function of the Refilin-Filamin complex to dynamic regulation of cell membrane remodelling., Competing Interests: The authors declare no competing or financial interests., (© 2016. Published by The Company of Biologists Ltd.)- Published
- 2016
- Full Text
- View/download PDF
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