Reconstitution of a Mg-ATP-dependent protein phosphatase and its activation through a phosphorylation mechanism

Brian A. Hemmings, Therese J. Resink, Philip Cohen

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    135 Citations (Scopus)

    Abstract

    A Mg-ATP-dependent protein phosphatase has been reconstituted from the catalytic subunit of protein phosphatase-1 and inhibitor-2, and consists of a 1:1 complex between these proteins. Activation of this enzyme by glycogen synthase kinase-3 and Mg-ATP results from the phosphorylation of inhibitor-2 on a threonine residue(s) and is accompanied by the dissociation of the complex. The results prove that protein phosphatase-1 and the Mg-ATP-dependent protein phosphatase contain the same catalytic subunit, and that they are interconvertible forms of the same enzyme.

    Original languageEnglish
    Pages (from-to)319-324
    Number of pages6
    JournalFEBS Letters
    Volume150
    Issue number2
    DOIs
    Publication statusPublished - 27 Dec 1982

    Keywords

    • Glycogen synthase kinase
    • Inhibitor-2
    • Phosphorylase
    • Protein phosphatase-1
    • Thiophosphorylation

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