Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin

Guillermo Velasco, Chris Armstrong, Nick Morrice, Sheelagh Frame, Philip Cohen

    Research output: Contribution to journalArticle

    167 Citations (Scopus)

    Abstract

    Rho kinase is known to control smooth muscle contractility by phosphorylating the 110 kDa myosin-targetting subunit (MYPT1) of the myosin-associated form of protein phosphatase 1 (PP1M). Phosphorylation of MYPT1 at Thr695 has previously been reported to inhibit the catalytic activity of PP1. Here, we show that the phosphorylation of Thr850 by Rho kinase dissociates PP1M from myosin, providing a second mechanism by which myosin phosphatase activity is inhibited.

    Original languageEnglish
    Pages (from-to)101-104
    Number of pages4
    JournalFEBS Letters
    Volume527
    Issue number1-3
    DOIs
    Publication statusPublished - 11 Sep 2002

    Fingerprint

    Phosphorylation
    Muscle Proteins
    Phosphoprotein Phosphatases
    Myosins
    Smooth Muscle
    rho-Associated Kinases
    Myosin-Light-Chain Phosphatase
    Protein Phosphatase 1
    Muscle
    Catalyst activity

    Keywords

    • Myosin
    • Protein phosphatase 1
    • Rho kinase
    • Smooth muscle

    Cite this

    Velasco, Guillermo ; Armstrong, Chris ; Morrice, Nick ; Frame, Sheelagh ; Cohen, Philip. / Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin. In: FEBS Letters. 2002 ; Vol. 527, No. 1-3. pp. 101-104.
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    Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin. / Velasco, Guillermo; Armstrong, Chris; Morrice, Nick; Frame, Sheelagh; Cohen, Philip.

    In: FEBS Letters, Vol. 527, No. 1-3, 11.09.2002, p. 101-104.

    Research output: Contribution to journalArticle

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    AU - Velasco, Guillermo

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    AU - Morrice, Nick

    AU - Frame, Sheelagh

    AU - Cohen, Philip

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