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Biochem Biophys Res Commun. 2011 Jun 24;410(1):87-90. doi: 10.1016/j.bbrc.2011.05.110. Epub 2011 May 27.

Study of the docking-dependent PLK1 phosphorylation of the CDC25B phosphatase.

Author information

1
Université de Toulouse, LBCMCP, F-31062 Toulouse, France.

Abstract

CDC25 (A, B and C) phosphatases control cell cycle progression through the timely dephosphorylation and activation of cyclin-dependent kinases (CDK). At mitosis the CDC25B phosphatase activity is dependent on its phosphorylation by multiple kinases impinging on its localisation, stability and catalytic activity. Here we report that prior phosphorylation of CDC25B by CDK1 enhances its substrate properties for PLK1 in vitro, and we also show that phosphorylated S50 serves as a docking site for PLK1. Using a sophisticated strategy based on the sequential phosphorylation of CDC25B with (16)O and (18)O ATP prior to nanoLC-MS/MS analysis we identified 13 sites phosphorylated by PLK1. This study illustrates the complexity of the phosphorylation pattern and of the subsequent regulation of CDC25B activity.

PMID:
21640712
DOI:
10.1016/j.bbrc.2011.05.110
[Indexed for MEDLINE]

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