[From ovocyte to biochemistry of the cell cycle].
The cell division cycle in eukaryotes contains up to three major transition points; the conversion of quiescent cells to a stage of active proliferation, the initiation of DNA synthesis (S phase) and the induction of mitosis in cells with newly replicated genome (M phase). Within the past years two strategies, have converged to identify, genetically and biochemically a key protein kinase p34 cdc2 that governs the entry into mitosis. In the fission yeast Schizosaccharomyces pombe a number of mutants in the mitotic regulatory circuit have been isolated. A central gene in the network is cdc2 which is essential for the proper execution of mitosis. The cdc2 gene interacts with a number of other genes for correct mitotic control. The Amphibian oocyte, the oocyte from Xenopus laevis particularly, is arrested at the G2 phase of the first meiotic division; when it enters M phase, it contains a dominant regulatory factor known as MPF (M-phase or maturation promoting factor). Purified MPF is an heterodimer formed of two polypeptides p34cdc2 an homologue of the product of the gene cdc2 and p45cdc13 or cyclin an homologue of the product of the gene cdc13. Biochemical studies have revealed that p34cdc2 is a phosphotyrosine protein during the G2 phase of the cell cycle, both mitotic and meiotic. The tyrosine phosphorylation of p34cdc2 is regulated by the gradual accumulation of cyclin. At the onset of M phase, the complex p34cdc2/cyclin is activated as an histone H1 kinase, and p34cdc2 is tyrosine dephosphorylated. The mechanism of activation of p34cdc2 is negatively regulated by a form of protein phosphatase 2A. Ovulated vertebrate oocytes are arrested at metaphase of the second meiotic division (M II) under the control of the proto-oncogene c-mos a protein kinase. The exit of M II phase and the initiation of early embryonic mitotic cell cycles are physiologically induced by the spermatozoa at the time of fertilization. They requires the degradation of c-mos by a Ca2+ dependent proteolytic enzyme and the destruction of cyclin by an ubiquitin dependent pathway. The Xenopus oocyte has led to the molecular elucidation of MPF and identified links between cell cycle control, protein phosphorylation and proto-oncogenes. Despite the impresive progess of recent years, there is still much to be learned about the control of meiosis in Xenopus oocytes.
Ozon
R
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Laboratoire de Physiologie de la Reproduction, INRA--CNRS URA 1449, Université Pierre et Marie Curie, Paris.
D000818:Animals; D016203:CDC2 Protein Kinase / Q000502:physiology; D002455:Cell Division; D000242:Cyclic AMP / Q000502:physiology; D016213:Cyclins / Q000096:biosynthesis; D011905:Genes, ras / Q000502:physiology; D006801:Humans; D016200:Maturation-Promoting Factor / Q000502:physiology; D008938:Mitosis; D009865:Oocytes / Q000737:chemistry* / Q000502:physiology; D010749:Phosphoprotein Phosphatases / Q000502:physiology; D010766:Phosphorylation; D054648:Protein Phosphatase 2; D000090063:Proto-Oncogene Mas; D012568:Schizosaccharomyces / Q000235:genetics
D016213:Cyclins; C000715470:MAS1 protein, human; D000090063:Proto-Oncogene Mas; D000242:Cyclic AMP; D016203:CDC2 Protein Kinase; D016200:Maturation-Promoting Factor; D010749:Phosphoprotein Phosphatases; D054648:Protein Phosphatase 2
De l'ovocyte à la biochimie du cycle cellulaire.