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• W2039144927 endingPage "16799" @default.
• W2039144927 startingPage "16794" @default.
• W2039144927 abstract "Xenopus oocytes, which are arrested in G(2) of meiosis I, contain complexes of cyclin B-cdc2 (M phase-promoting factor) that are kept repressed by inhibitory phosphorylations on cdc2 at Thr-14 and Tyr-15. Progesterone induces a cytoplasmic signaling pathway that leads to activation of cdc25, the phosphatase that removes these phosphorylations, catalyzing entry into M phase. It has been known for 25 years that high levels of cAMP and protein kinase A (PKA) are required to maintain the G(2) arrest and that a drop in PKA activity is required for M phase-promoting factor activation, but no physiological targets of PKA have been identified. We present evidence that cdc25 is a critical target of PKA. (i) In vitro, cdc25 Ser-287 serves as a major site of phosphorylation by PKA, resulting in sequestration by 14-3-3. (ii) Endogenous cdc25 is phosphorylated on Ser-287 in oocytes and dephosphorylated in response to progesterone just before cdc2 dephosphorylation and M-phase entry. (iii) High PKA activity maintains phosphorylation of Ser-287 in vivo, whereas inhibition of PKA by its heat-stable inhibitor (PKI) induces dephosphorylation of Ser-287. (iv) Overexpression of mutant cdc25 (S287A) bypasses the ability of PKA to maintain oocytes in G(2) arrest. These findings argue that cdc25 is a physiologically relevant target of PKA in oocytes. In the early embryonic cell cycles, Ser-287 is phosphorylated during interphase and dephosphorylated just before cdc2 activation and mitotic entry. Thus, in addition to its role in checkpoint arrest, cdc25 Ser-287 serves as a site for regulation during normal, unperturbed cell cycles." @default.
• W2039144927 created "2016-06-24" @default.
• W2039144927 creator A5011547009 @default.
• W2039144927 creator A5040169264 @default.
• W2039144927 creator A5059252054 @default.
• W2039144927 date "2002-12-11" @default.
• W2039144927 modified "2023-09-30" @default.
• W2039144927 title "G ₂ arrest in <i>Xenopus</i> oocytes depends on phosphorylation of cdc25 by protein kinase A" @default.
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• W2039144927 doi "https://doi.org/10.1073/pnas.222661299" @default.
• W2039144927 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/139223" @default.
• W2039144927 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12477927" @default.
• W2039144927 hasPublicationYear "2002" @default.
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