Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14-3-3 binding
Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14-3-3 binding
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DOI：
10.1016/s0014-5793(02)03327-6
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发表时间：
2002-09-25
期刊：
影响因子：
3.5
通讯作者：
Clarke, PR
中科院分区：
文献类型：
--
作者：
Hutchins, JRA;Dikovskaya, D;Clarke, PR
Cdc25C phosphatase induces mitosis by dephosphorylating and activating Cdc2/cyclin B protein kinase. Phosphorylation of Xenopus Cdc25C at serine 287 creates a binding site for a 14-3-3 protein and restrains activation during interphase. Here, we show that dephosphorylation of S287 is catalysed by protein phosphatase-2A in Xenopus egg extracts. 14-3-3 protein binding to Cdc25C inhibits dephosphorylation of S287, providing a mechanism to maintain phospborylation of that site during interphase. The rate of dephosphorylation of S287 is not increased in mitotic extracts, indicating that the phosphorylation status of the site is likely to be controlled through modulation of kinases or 14-3-3 binding activity. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
