Cdc2-Cyclin B Triggers H3 Kinase Activation of Aurora-A in Xenopus Oocytes
Autor: | Catherine Jessus, Thierry Lorca, Claude Prigent, Catherine Thibier, Anna Castro, Gilliane Maton |
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Přispěvatelé: | Laboratoire de Biologie du Développement (LBD), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), 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)-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), Centre de recherches de biochimie macromoléculaire (CRBM), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-IFR122-Centre National de la Recherche Scientifique (CNRS), 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), Institut de la Recherche Agronomique, CNRS, University of Paris VI and Paris XI, Association pour la Recherche Contre le Cancer (Grant 4771) and Ligue Nationale Contre le Cancer (to C. J. and T. L.)., 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), Université de Rennes (UR)-IFR97-Centre National de la Recherche Scientifique (CNRS), Laboratoire associé de physiologie de la reproduction, Institut National de la Recherche Agronomique (INRA)-Université Pierre et Marie Curie - Paris 6 (UPMC), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Recherche Agronomique (INRA), Centre National de la Recherche Scientifique (CNRS)-IFR122-Université Montpellier 2 - Sciences et Techniques (UM2)-Université Montpellier 1 (UM1), Prigent, Claude |
Rok vydání: | 2003 |
Předmět: |
MESH: Signal Transduction
MAPK/ERK pathway protéine kinase Time Factors cycline Xenopus [SDV]Life Sciences [q-bio] Cyclin B Cell Cycle Proteins Xenopus Proteins Biochemistry Histones MESH: Recombinant Proteins 0302 clinical medicine Aurora Kinases MESH: cdc25 Phosphatases MESH: Progesterone Cyclic AMP MESH: Up-Regulation MESH: Animals MESH: Xenopus Phosphorylation MESH: Xenopus Proteins Progesterone ComputingMilieux_MISCELLANEOUS MESH: Cyclic AMP MESH: Histones 0303 health sciences MESH: Kinetics MESH: Peptides Kinase ovocyte MESH: CDC2 Protein Kinase Recombinant Proteins Up-Regulation Cell biology Meiosis 030220 oncology & carcinogenesis embryonic structures MESH: Phosphoric Monoester Hydrolases biological phenomena cell phenomena and immunity Signal transduction Signal Transduction Cyclin-Dependent Kinase Inhibitor p21 méiose MESH: Enzyme Activation Blotting Western Mitosis Spindle Apparatus [SDV.BC]Life Sciences [q-bio]/Cellular Biology Protein Serine-Threonine Kinases Biology MESH: Protein-Serine-Threonine Kinases MESH: Cyclin-Dependent Kinase Inhibitor p21 MESH: Oocytes MESH: Aurora Kinases 03 medical and health sciences MESH: Cell Cycle Proteins Cyclins CDC2 Protein Kinase Animals cdc25 Phosphatases MESH: Blotting Western Kinase activity MESH: Spindle Apparatus [SDV.BC] Life Sciences [q-bio]/Cellular Biology MESH: Protein Kinases Molecular Biology 030304 developmental biology Cyclin-dependent kinase 1 MESH: Phosphorylation maturation urogenital system MESH: Time Factors MESH: Cyclin B Cell Biology MESH: Mitosis MESH: Cyclins biology.organism_classification Phosphoric Monoester Hydrolases Spindle apparatus Enzyme Activation Kinetics MESH: Meiosis xenope Oocytes biology.protein Peptides Protein Kinases |
Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2003, 278 (24), pp.21439-49. ⟨10.1074/jbc.M300811200⟩ Journal of Biological Chemistry, 2003, 278 (24), pp.21439-49. ⟨10.1074/jbc.M300811200⟩ Journal of Biological Chemistry, 2003, 278 (24), pp.21439-21449 Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2003, 278 (24), pp.21439-21449 Journal of Biological Chemistry 24 (278), 21439-21449. (2003) |
ISSN: | 0021-9258 1083-351X |
Popis: | International audience; Xenopus oocytes are arrested in meiotic prophase I and resume meiotic divisions in response to progesterone. Progesterone triggers activation of M-phase promoting factor (MPF) or Cdc2-cyclin B complex and neosynthesis of Mos kinase, responsible for MAPK activation. Both Cdc2 and MAPK activities are required for the success of meiotic maturation. However, the signaling pathway induced by progesterone and leading to MPF activation is poorly understood, and most of the targets of both Cdc2 and MAPK in the oocyte remain to be determined. Aurora-A is a Ser/Thr kinase involved in separation of centrosomes and in spindle assembly during mitosis. It has been proposed that in Xenopus oocytes Aurora-A could be an early component of the progesterone-transduction pathway, acting through the regulation of Mos synthesis upstream Cdc2 activation. We addressed here the question of Aurora-A regulation during meiotic maturation by using new in vitro and in vivo experimental approaches. We demonstrate that Cdc2 kinase activity is necessary and sufficient to trigger both Aurora-A phosphorylation and kinase activation in Xenopus oocyte. In contrast, these events are independent of the Mos/MAPK pathway. Aurora-A is phosphorylated in vivo at least on three residues that regulate differentially its kinase activity. Therefore, Aurora-A is under the control of Cdc2 in the Xenopus oocyte and could be involved in meiotic spindle establishment. |
Databáze: | OpenAIRE |
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