Phosphorylation of CDC25C at S263 controls its intracellular localisation
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- 作者：Charlotte Esmenjaud-Mailhat ; Valé ; rie Lobjois ; Carine Froment ; Roy M. Golsteyn ; Bernard Monsarrat ; Bernard Ducommun
- 关键词：CDC25C ; Phosphorylation ; Mitosis ; Cell cycle
- 刊名：FEBS Letters
- 出版年：2007
- 出版时间：21 August 2007
- 年：2007
- 卷：581
- 期：21
- 页码：3979-3985
- 全文大小：707 K
文摘
CDC25C phosphatase is a key actor in cell cycle progression that controls the activation of CDK1-cyclin B at mitosis. Its activity is known to be highly regulated by a number of signalling pathway-activated kinases resulting in its phosphorylation on multiple residues. In this study, we have purified CDC25C from cells and have used a proteomic approach to identify new regulatory phosphorylations. Here, we report the identification by mass spectrometry of a peptide monophosphorylated on serine 263. We demonstrate by cell imaging that mutation of S263 to alanine leads to a nuclear accumulation of CDC25C that is further reinforced by leptomycin-B. We propose that phosphorylation at S263 is part of the regulatory mechanism that modulates nuclear import of CDC25C, thus preventing cytoplasm to nucleus shuttling.