8 results on '"Andrieux, Annie"'
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2. MAP6-F Is a Temperature Sensor That Directly Binds to and Protects Microtubules from Cold-induced Depolymerization
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Delphin, Christian, Bouvier, Denis, Seggio, Maxime, Couriol, Emilie, Saoudi, Yasmina, Denarier, Eric, Bosc, Christophe, Valiron, Odile, Bisbal, Mariano, Arnal, Isabelle, and Andrieux, Annie
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- 2012
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3. Post-translational Arginylation of Calreticulin: A NEW ISOSPECIES OF CALRETICULIN COMPONENT OF STRESS GRANULES
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Decca, María B., Carpio, Marcos A., Bosc, Christophe, Galiano, Mauricio R., Job, Didier, Andrieux, Annie, and Hallak, Marta E.
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- 2007
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4. STOP-like Protein 21 Is a Novel Member of the STOP Family, Revealing a Golgi Localization of STOP Proteins
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Gory-Fauré, Sylvie, Windscheid, Vanessa, Bosc, Christophe, Peris, Leticia, Proietto, Dominique, Franck, Ronald, Denarier, Eric, Job, Didier, and Andrieux, Annie
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- 2006
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5. Phosphorylation of Microtubule-associated Protein STOP by Calmodulin Kinase II
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Baratier, Julie, Peris, Leticia, Brocard, Jacques, Gory-Fauré, Sylvie, Dufour, Fabrice, Bosc, Christophe, Fourest-Lieuvin, Anne, Blanchoin, Laurent, Salin, Paul, Job, Didier, and Andrieux, Annie
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- 2006
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6. The Ecto-enzyme CD38 Is a Nicotinic Acid Adenine Dinucleotide Phosphate (NAADP) Synthase That Couples Receptor Activation to Ca2+ Mobilization from Lysosomes in Pancreatic Acinar Cells
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José-Manuel Cancela, Frances E. Lund, Nathalie Cheviron, Michiko Yamasaki, Alexis Menteyne, François Cosker, Marie-Jo Moutin, Antony Galione, Laboratoire de neurobiologie cellulaire et moléculaire (NBCM), Centre National de la Recherche Scientifique (CNRS), Institut de Neurobiologie Alfred Fessard (INAF), Department of Pharmacology, University of Oxford [Oxford], Department of Medicine, Division of Allergy, Immunology, and Rheumatology, University of Rochester [USA], The Trudeau Institute, Grenoble Institut des Neurosciences (GIN), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), CNRS, ARC, AFM, Andrieux, Annie, and University of Oxford
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Cholagogues and Choleretics ,MESH: Membrane Glycoproteins ,CD38 ,MESH: Mice, Knockout ,Biochemistry ,Mice ,chemistry.chemical_compound ,0302 clinical medicine ,MESH: Nucleotidyltransferases ,MESH: Animals ,MESH: Cholagogues and Choleretics ,MESH: Cholecystokinin ,Cholecystokinin ,Mice, Knockout ,0303 health sciences ,Membrane Glycoproteins ,Nucleotidyltransferases ,Pancreas, Exocrine ,MESH: Calcium ,Signal transduction ,MESH: NADP ,Intracellular ,Signal Transduction ,ADP-ribosyl Cyclase ,MESH: Rats ,Endosome ,Biology ,MESH: Calcium Signaling ,Cell Line ,03 medical and health sciences ,[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Animals ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Secretion ,Calcium Signaling ,MESH: Pancreas, Exocrine ,MESH: Mice ,Molecular Biology ,030304 developmental biology ,Nicotinic acid adenine dinucleotide phosphate ,MESH: Antigens, CD38 ,Cell Biology ,ADP-ribosyl Cyclase 1 ,Rats ,MESH: Cell Line ,chemistry ,Calcium ,Lysosomes ,NADP ,030217 neurology & neurosurgery ,MESH: Lysosomes - Abstract
International audience; Nicotinic acid adenine dinucleotide phosphate (NAADP) is the most potent Ca(2+)-mobilizing intracellular messenger and is linked to a variety of stimuli and cell surface receptors. However, the enzyme responsible for endogenous NAADP synthesis in vivo is unknown, and it has been proposed that another enzyme differing from ADP-ribosyl cyclase family members may exist. The ecto-enzyme CD38, involved in many functions as diverse as cell proliferation and social behavior, represents an important alternative. In pancreatic acinar cells, the hormone cholecystokinin (CCK) stimulates NAADP production evoking Ca(2+) signals by discharging acidic Ca(2+) stores and leading to digestive enzyme secretion. From cells derived from CD38(-/-) mice, we provide the first physiological evidence that CD38 is required for endogenous NAADP generation in response to CCK stimulation. Furthermore, CD38 expression in CD38-deficient pancreatic AR42J cells remodels Ca(2+)-signaling pathways in these cells by restoring Ca(2+) mobilization from lysosomes during CCK-induced Ca(2+) signaling. In agreement with an intracellular site for messenger synthesis, we found that CD38 is expressed in endosomes. These CD38-containing vesicles, likely of endosomal origin, appear to be proximal to lysosomes but not co-localized with them. We propose that CD38 is an NAADP synthase required for coupling receptor activation to NAADP-mediated Ca(2+) release from lysosomal stores in pancreatic acinar cells.
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- 2010
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7. A Single Residue in a Novel ADP-ribosyl Cyclase Controls Production of the Calcium-mobilizing Messengers Cyclic ADP-ribose and Nicotinic Acid Adenine Dinucleotide Phosphate
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Marie-Jo Moutin, Hélène Muller-Steffner, Latha Ramakrishnan, Leslie Dale, Sandip Patel, Christophe Bosc, Francis Schuber, Victor D. Vacquier, Department of Cell and Developmental Biology, University College of London [London] (UCL), Faculté de Pharmacie, Groupe Physiopathologie du Cytosquelette (GPC), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), 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)-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)-Institut National de la Santé et de la Recherche Médicale (INSERM), Marine Biology Research Division, University of California [San Diego] (UC San Diego), University of California-University of California-Scripps Institution of Oceanography, Grants BB/D018110/1 and BB/G013721/1 from the Biotechnology and Biological Sciences Research Council (to S.P.). PhD studentship from the Medical Research Council (to L.R.)., Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Scripps Institution of Oceanography (SIO - UC San Diego), University of California (UC)-University of California (UC)-University of California [San Diego] (UC San Diego), University of California (UC)-University of California (UC), and Andrieux, Annie
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ADP-ribosyl Cyclase ,Blastomeres ,Microinjections ,Blotting, Western ,Molecular Sequence Data ,Multifunctional Enzymes ,Biology ,Transfection ,Biochemistry ,Cyclic ADP-ribose ,Cyclase ,Cell Line ,Xenopus laevis ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Animals ,Humans ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Amino Acid Sequence ,Cloning, Molecular ,Tyrosine ,Strongylocentrotus purpuratus ,Molecular Biology ,030304 developmental biology ,Cyclic ADP-Ribose ,0303 health sciences ,Microscopy, Confocal ,Nicotinic acid adenine dinucleotide phosphate ,Sequence Homology, Amino Acid ,Inositol trisphosphate ,Cell Biology ,Kinetics ,chemistry ,Mutation ,NAD+ kinase ,NADP ,030217 neurology & neurosurgery ,Signal Transduction - Abstract
International audience; Cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate are ubiquitous calcium-mobilizing messengers produced by the same family of multifunctional enzymes, the ADP-ribosyl cyclases. Not all ADP-ribosyl cyclases have been identified, and how production of different messengers is achieved is incompletely understood. Here, we report the cloning and characterization of a novel ADP-ribosyl cyclase (SpARC4) from the sea urchin, a key model organism for the study of calcium-signaling pathways. Like several other members of the ADP-ribosyl cyclase superfamily, SpARC4 is a glycoprotein targeted to the plasma membrane via a glycosylphosphatidylinositol anchor. However, unlike most other members, SpARC4 shows a remarkable preference for producing cyclic ADP-ribose over nicotinic acid adenine dinucleotide phosphate. Mutation of a single residue (tyrosine 142) within a noncanonical active site reversed this striking preference. Our data highlight further diversification of this unusual enzyme family, provide mechanistic insight into multifunctionality, and suggest that different ADP-ribosyl cyclases are fine-tuned to produce specific calcium-mobilizing messengers.
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- 2010
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8. S-Trityl-L-cysteine Is a Reversible, Tight Binding Inhibitor of the Human Kinesin Eg5 That Specifically Blocks Mitotic Progression
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Richard H. Wade, Luc Lebeau, Dimitrios A. Skoufias, Robert A. Cross, Yasmina Saoudi, Isabelle Crevel, Salvatore DeBonis, Frank Kozielski, David D. Hackney, Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), 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)-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)-Centre National de la Recherche Scientifique (CNRS), Organisation Fonctionnelle du Cytosquelette, Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR27, Institut Gilbert-Laustriat : Biomolécules, Biotechnologie, Innovation Thérapeutique, Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Marie Curie Research Institute, MRCI, Department of Biological Sciences [Pittsburgh], Carnegie Mellon University [Pittsburgh] (CMU), This work was supported by Contract 5197 from Association pour la Recherche sur le Cancer, Alliance Des Recherches sur le Cancer, and Contracts 03 013690 02 and 03 013690 01 from the Re´gion Rhoˆ ne-Alpes. The costs of publication of this article were defrayed in part by the payment of page charges., Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Conception et application de molécules bioactives (CAMB), Université de Strasbourg (UNISTRA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), The Beatson Institute for Cancer Research, University of Glasgow, and Andrieux, Annie
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MESH: Osteosarcoma ,[SDV]Life Sciences [q-bio] ,Kinesins ,MESH: Drug Design ,Biochemistry ,MESH: Recombinant Proteins ,MESH: Protein Structure, Tertiary ,chemistry.chemical_compound ,0302 clinical medicine ,ortho-Aminobenzoates ,MESH: Animals ,ComputingMilieux_MISCELLANEOUS ,Osteosarcoma ,0303 health sciences ,MESH: Anthranilic Acids ,Stereoisomerism ,Cell cycle ,Microtubule sliding ,MESH: Bone Neoplasms ,Recombinant Proteins ,Cell biology ,Adenosine Diphosphate ,MESH: Cattle ,Monastrol ,030220 oncology & carcinogenesis ,MESH: Cell Division ,Kinesin ,Cell Division ,Protein Binding ,Mitosis ,Bone Neoplasms ,Spindle Apparatus ,[SDV.BC]Life Sciences [q-bio]/Cellular Biology ,Biology ,03 medical and health sciences ,[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology ,[CHIM]Chemical Sciences ,Animals ,Humans ,MESH: Protein Binding ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Cysteine ,[SDV.BC] Life Sciences [q-bio]/Cellular Biology ,Molecular Biology ,030304 developmental biology ,MESH: Mitotic Spindle Apparatus ,MESH: Humans ,MESH: Adenosine Diphosphate ,Cell Biology ,MESH: Mitosis ,MESH: Cysteine ,MESH: Stereoisomerism ,Protein Structure, Tertiary ,Spindle apparatus ,MESH: Hela Cells ,chemistry ,Centrosome ,Cell culture ,Drug Design ,Cattle ,MESH: Kinesin ,HeLa Cells - Abstract
International audience; Human Eg5, responsible for the formation of the bipolar mitotic spindle, has been identified recently as one of the targets of S-trityl-L-cysteine, a potent tumor growth inhibitor in the NCI 60 tumor cell line screen. Here we show that in cell-based assays S-trityl-L-cysteine does not prevent cell cycle progression at the S or G(2) phases but inhibits both separation of the duplicated centrosomes and bipolar spindle formation, thereby blocking cells specifically in the M phase of the cell cycle with monoastral spindles. Following removal of S-trityl-L-cysteine, mitotically arrested cells exit mitosis normally. In vitro, S-trityl-L-cysteine targets the catalytic domain of Eg5 and inhibits Eg5 basal and microtubule-activated ATPase activity as well as mant-ADP release. S-trityl-L-cysteine is a tight binding inhibitor (estimation of K(i,app)
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- 2006
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