Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14-3-3 binding

James R.A. Hutchins, Dina Dikovskaya, Paul R. Clarke

    Research output: Contribution to journalArticlepeer-review

    22 Citations (Scopus)

    Abstract

    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 phosphorylation 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.

    Original languageEnglish
    Pages (from-to)267-271
    Number of pages5
    JournalFEBS Letters
    Volume528
    Issue number1-3
    DOIs
    Publication statusPublished - 25 Sept 2002

    Keywords

    • 14-3-3 protein
    • Cdc25
    • Cell cycle checkpoint
    • Chk1
    • Protein phosphatase

    ASJC Scopus subject areas

    • Structural Biology
    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Genetics
    • Cell Biology

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