Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines

Dario R Alessi, Nestor Gomez, Greg Moorhead, Tom Lewis, Stephen M Keyse, Philip Cohen

    Research output: Contribution to journalArticle

    315 Citations (Scopus)

    Abstract

    Mitogen-activated protein (MAP) kinase is central to a signal transduction pathway that triggers cell proliferation or differentiation. Activation of the p42mapk isoform requires its phosphorylation at two residues, Thr 183 and Tyr 185, and this phosphorylation is catalysed by MAP kinase kinase (MAPKK). Relatively little is known, however, about the enzymes that dephosphorylate these residues, thereby inactivating the pathway. Recently, the CL100 phosphatase has been shown to inactivate p42mapk in vitro by dephosphorylating Thr 183 and Tyr 185 at similar rates. CL100, the product of an immediate early gene, is synthesized within one hour of stimulating cells with growth factors or exposure to oxidative stress or heat shock. Incubation of NIH 3T3 fibroblasts with cycloheximide prevents both synthesis of CL100 and inactivation of p42mapk after stimulation with serum.
    Original languageEnglish
    Pages (from-to)283-95
    Number of pages13
    JournalCurrent Biology
    Volume5
    Issue number3
    DOIs
    Publication statusPublished - 1995

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