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
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