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Phosphorylation of CDC25C at S263 controls its intracellular localisation
Author(s) -
Esmenjaud-Mailhat Charlotte,
Lobjois Valérie,
Froment Carine,
Golsteyn Roy M.,
Monsarrat Bernard,
Ducommun Bernard
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.07.024
Subject(s) - phosphorylation , cyclin dependent kinase 1 , serine , kinase , microbiology and biotechnology , nuclear export signal , mitosis , phosphatase , nuclear transport , cytoplasm , protein serine threonine kinases , biochemistry , biology , cell cycle , chemistry , cell nucleus , cell , protein kinase a
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.