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2 results on '"Gladys Mirey"'

1. Phosphorylation of CDC25B by Aurora-A at the centrosome contributes to the G2–M transition

Author

Bernard Monsarrat, Gladys Mirey, Nathalie Theis-Febvre, Estelle Schmitt, Stéphanie Dutertre, Carine Froment, Jean-Pierre Bouché, Martine Cazales, Christine Dozier, Bernard Ducommun, Muriel Quaranta, Valerie Trabut, Claude Prigent, Génétique et Développement, Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-IFR97-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie Cellulaire et Moléculaire du Contrôle de la Prolifération (LBCMCP), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Ducommun, Bernard, Université de Rennes (UR)-IFR97-Centre National de la Recherche Scientifique (CNRS), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), and Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Time Factors, Cell Cycle Proteins, Centrosome cycle, Xenopus Proteins, MESH: Microinjections, Aurora-A, MESH: Centrosome, MESH: Antibodies, Monoclonal, 0302 clinical medicine, MESH: cdc25 Phosphatases, Aurora Kinases, Serine, Phosphorylation, MESH: Xenopus Proteins, 0303 health sciences, Kinase, Antibodies, Monoclonal, Cell biology, 030220 oncology & carcinogenesis, MESH: Cell Division, RNA Interference, biological phenomena, cell phenomena, and immunity, Cell Division, Autre (Sciences du Vivant), CDC25B phosphatase, G2 Phase, Microinjections, MESH: RNA Interference, centrosome, mitosis, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, macromolecular substances, Protein Serine-Threonine Kinases, Biology, MESH: Protein-Serine-Threonine Kinases, Antibodies, 03 medical and health sciences, MESH: Cell Cycle Proteins, Cyclin-dependent kinase, Humans, cdc25 Phosphatases, MESH: Serine, Protein kinase A, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, MESH: Protein Kinases, Mitosis, 030304 developmental biology, Centrosome, MESH: Humans, MESH: Phosphorylation, MESH: Antibodies, MESH: Time Factors, G1/S transition, Cell Biology, MESH: Hela Cells, MESH: G2 Phase, enzymes and coenzymes (carbohydrates), biology.protein, Cancer research, Protein Kinases, HeLa Cells
Abstract

Aurora-A protein kinase, which is the product of an oncogene, is required for the assembly of a functional mitotic apparatus and the regulation of cell ploidy. Overexpression of Aurora-A in tumour cells has been correlated with cancer susceptibility and poor prognosis. Aurora-A activity is required for the recruitment of CDK1-cyclin B1 to the centrosome prior to its activation and the commitment of the cell to mitosis. In this report, we demonstrate that the CDC25B phosphatase, an activator of cyclin dependent kinases at mitosis, is phosphorylated both in vitro and in vivo by Aurora-A on serine 353 and that this phosphorylated form of CDC25B is located at the centrosome during mitosis. Knockdown experiments by RNAi confirm that the centrosome phosphorylation of CDC25B on S353 depends on Aurora-A kinase. Microinjection of antibodies against phosphorylated S353 results in a mitotic delay whilst overexpression of a S353 phosphomimetic mutant enhances the mitotic inducing effect of CDC25B. Our results demonstrate that Aurora-A phosphorylates CDC25B in vivo at the centrosome during mitosis. This phosphorylation might locally participate in the control of the onset of mitosis. These findings re-emphasise the role of the centrosome as a functional integrator of the pathways contributing to the triggering of mitosis.

Published
2004

2. RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex: involvement of the Ral pathway in receptor endocytosis

Author

Jacques Camonis, Yannick Mahé, B. Meunier-Bisceuil, A. Sorkin, Corinne Leprince, Gladys Mirey, V. Jullien-Flores, Transduction du signal et oncogénèse, Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Génotoxicité & Signalisation (ToxAlim-GS), ToxAlim (ToxAlim), Institut National de la Recherche Agronomique (INRA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Recherche Agronomique (INRA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, University of Colorado, University of Colorado [Boulder], and ProdInra, Migration

Subjects
GTPase-activating protein, GTP Phosphohydrolases, 0302 clinical medicine, Epidermal growth factor, Genes, Reporter, RLIP76, 0303 health sciences, RALB, Ras signalling, GTPase-Activating Proteins, Transferrin, Signal transducing adaptor protein, RALA, Endocytosis, Cell biology, Adaptor Protein Complex mu Subunits, ErbB Receptors, 030220 oncology & carcinogenesis, Signal transduction, Protein Binding, Signal Transduction, [SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT], animal structures, Adaptor Protein Complex 3, Adaptor Protein Complex 1, Green Fluorescent Proteins, Adaptor Protein Complex 2, Biology, Transfection, Evolution, Molecular, 03 medical and health sciences, Adaptor Protein Complex alpha Subunits, Two-Hybrid System Techniques, Receptors, Transferrin, Humans, 030304 developmental biology, adaptin, Epidermal Growth Factor, [SDV.OT] Life Sciences [q-bio]/Other [q-bio.OT], Membrane Proteins, Epithelial Cells, Cell Biology, Ral, Adaptor Proteins, Vesicular Transport, Luminescent Proteins, Ral GTP-Binding Proteins, Mutagenesis, ras Proteins, ATP-Binding Cassette Transporters, Indicators and Reagents, ral GTP-Binding Proteins, Carrier Proteins, Gene Deletion, HeLa Cells
Abstract

International audience; RLIP76 is a modular protein that was identified as a putative effector of Ral, a GTPase activated during Ras signaling. To explore further the contribution of the Ral-RLIP76 pathway to Ras signaling, we have looked for partners of RLIP76. Mu2, the medium chain of the AP2 complex is shown to interact with RLIP76. We show also that in vivo endogenous AP2 and RLIP76 form a complex and that this in vivo interaction is independent of cells being stimulated by a growth factor. Furthermore, RLIP76 differentiates AP2 from AP1 in vivo as RLIP76 differentiates mu2 from mu1 in vitro and in two hybrid assays. We show that activated Ral interferes with both tranferrin receptor endocytosis and epidermal growth factor (EGF) receptor endocytosis in HeLa cells. We propose a model where the Ral-RLIP76 pathway connects signal transduction and endocytosis through interaction on one hand between the Ras-Ral pathway and RLIP, on the other hand between RLIP and proteins belonging to the endocytotic machinery.

Published
2000

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