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Since almost two decades, it is known that progesterone is responsible of the release of the prophase I arrest of amphibian oocytes and leads to the activation of the universal MPF, through a puzzling transduction pathway. It involves negative regulation of the cAMP-dependent protein kinase (PKA) and synthesis of new proteins, among them the c-Mos protooncogene product. The implication of the Mos/mitogenic activated protein kinase (MAP kinase) pathway in Cdc2 activation has been extensively studied and is now at the centre of a controversial debate. In this paper, we discuss the current progress and our recent results on the molecular mechanisms allowing progesterone to activate MPF and propose a model to partly resolve the long-standing inconsistencies concerning the role of Mos/MAP kinase during this process.
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Karaı̈skou et al. (2001) studied this question.
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