YIL113w encodes a functional dual-specificity protein phosphatase which specifically interacts with and inactivates the Slt2/Mpk1p MAP kinase in S. cerevisiae

Michelle Collister, Mark P. Didmon, Fiona MacIsaac, Michael J. Stark, Neil Q. MacDonald, Stephen M. Keyse

    Research output: Contribution to journalArticle

    30 Citations (Scopus)

    Abstract

    We show here that the YIL113w gene of Saccharomyces cerevisiae encodes a functional protein phosphatase. Yil113p shows no activity in vitro towards either phosphorylated casein or myelin basic protein. However, Yil113p dephosphorylates activated extracellular signal-regulated kinase 2 MAP kinase indicating that it is a dual-specificity MAP kinase phosphatase. In support of this we find that Yil113p specifically interacts with the stress-activated Slt2/Mpk1p MAP kinase of S. cerevisiae. Furthermore, expression of Yil113p causes the dephosphorylation of Slt2/Mpk1p in vivo, while expression of an inactive mutant of Yil113p causes the accumulation of phosphorylated Slt2/Mpk1p. We conclude that the physiological target of YIL113p is Slt2/Mpk1p.
    Original languageEnglish
    Pages (from-to)186-92
    Number of pages7
    JournalFEBS Letters
    Volume527
    Issue number1-3
    DOIs
    Publication statusPublished - 11 Sep 2002

    Keywords

    • Signalling
    • DEPHOSPHORYLATION
    • Cell integrity
    • Stress response
    • SDP1

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