The major myosin phosphatase in skeletal muscle is a complex between the β-isoform of protein phosphatase 1 and the MYPT2 gene product

Greg Moorhead, Deborah Johnson, Nick Morrice, Philip Cohen

    Research output: Contribution to journalArticle

    43 Citations (Scopus)

    Abstract

    Myosin is dephosphorylated by distinct forms of protein phosphatase 1 (PP1) in smooth muscle and skeletal muscle that are composed of PP1 complexed to different regulatory subunits. The smooth muscle myosin phosphatase (smPP1M) has been characterised previously and is composed of PP1β complexed to M110 and M21 subunits that enhance the dephosphorylation of smooth muscle myosin, but not skeletal muscle myosin. In contrast, the regulatory subunit(s) of skeletal muscle myosin phosphatase (skPP1M) greatly enhance(s) the dephosphorylation of skeletal muscle myosin. Here we identify a regulatory subunit of skPP1M as the product of the MYPT2 gene, a protein whose sequence is 61% identical to the M110 subunit of smPP1M. Surprisingly, the M21 subunit of smPP1M appears to be produced from the same gene that encodes MYPT2. Copyright (C) 1998 Federation of European Biochemical Societies.

    Original languageEnglish
    Pages (from-to)141-144
    Number of pages4
    JournalFEBS Letters
    Volume438
    Issue number3
    DOIs
    Publication statusPublished - 6 Nov 1998

    Fingerprint

    Myosin-Light-Chain Phosphatase
    Skeletal Muscle Myosins
    Protein Phosphatase 1
    Smooth Muscle Myosins
    Muscle
    Protein Isoforms
    Skeletal Muscle
    Genes
    Muscle Proteins
    Myosins
    Smooth Muscle
    Proteins

    Keywords

    • Muscle contraction
    • Myosin
    • Protein phosphatase 1

    Cite this

    @article{4589db8211de4f12b9bb057f54d1b7ae,
    title = "The major myosin phosphatase in skeletal muscle is a complex between the β-isoform of protein phosphatase 1 and the MYPT2 gene product",
    abstract = "Myosin is dephosphorylated by distinct forms of protein phosphatase 1 (PP1) in smooth muscle and skeletal muscle that are composed of PP1 complexed to different regulatory subunits. The smooth muscle myosin phosphatase (smPP1M) has been characterised previously and is composed of PP1β complexed to M110 and M21 subunits that enhance the dephosphorylation of smooth muscle myosin, but not skeletal muscle myosin. In contrast, the regulatory subunit(s) of skeletal muscle myosin phosphatase (skPP1M) greatly enhance(s) the dephosphorylation of skeletal muscle myosin. Here we identify a regulatory subunit of skPP1M as the product of the MYPT2 gene, a protein whose sequence is 61{\%} identical to the M110 subunit of smPP1M. Surprisingly, the M21 subunit of smPP1M appears to be produced from the same gene that encodes MYPT2. Copyright (C) 1998 Federation of European Biochemical Societies.",
    keywords = "Muscle contraction, Myosin, Protein phosphatase 1",
    author = "Greg Moorhead and Deborah Johnson and Nick Morrice and Philip Cohen",
    year = "1998",
    month = "11",
    day = "6",
    doi = "10.1016/S0014-5793(98)01276-9",
    language = "English",
    volume = "438",
    pages = "141--144",
    journal = "FEBS Letters",
    issn = "0014-5793",
    publisher = "Wiley",
    number = "3",

    }

    The major myosin phosphatase in skeletal muscle is a complex between the β-isoform of protein phosphatase 1 and the MYPT2 gene product. / Moorhead, Greg; Johnson, Deborah; Morrice, Nick; Cohen, Philip.

    In: FEBS Letters, Vol. 438, No. 3, 06.11.1998, p. 141-144.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - The major myosin phosphatase in skeletal muscle is a complex between the β-isoform of protein phosphatase 1 and the MYPT2 gene product

    AU - Moorhead, Greg

    AU - Johnson, Deborah

    AU - Morrice, Nick

    AU - Cohen, Philip

    PY - 1998/11/6

    Y1 - 1998/11/6

    N2 - Myosin is dephosphorylated by distinct forms of protein phosphatase 1 (PP1) in smooth muscle and skeletal muscle that are composed of PP1 complexed to different regulatory subunits. The smooth muscle myosin phosphatase (smPP1M) has been characterised previously and is composed of PP1β complexed to M110 and M21 subunits that enhance the dephosphorylation of smooth muscle myosin, but not skeletal muscle myosin. In contrast, the regulatory subunit(s) of skeletal muscle myosin phosphatase (skPP1M) greatly enhance(s) the dephosphorylation of skeletal muscle myosin. Here we identify a regulatory subunit of skPP1M as the product of the MYPT2 gene, a protein whose sequence is 61% identical to the M110 subunit of smPP1M. Surprisingly, the M21 subunit of smPP1M appears to be produced from the same gene that encodes MYPT2. Copyright (C) 1998 Federation of European Biochemical Societies.

    AB - Myosin is dephosphorylated by distinct forms of protein phosphatase 1 (PP1) in smooth muscle and skeletal muscle that are composed of PP1 complexed to different regulatory subunits. The smooth muscle myosin phosphatase (smPP1M) has been characterised previously and is composed of PP1β complexed to M110 and M21 subunits that enhance the dephosphorylation of smooth muscle myosin, but not skeletal muscle myosin. In contrast, the regulatory subunit(s) of skeletal muscle myosin phosphatase (skPP1M) greatly enhance(s) the dephosphorylation of skeletal muscle myosin. Here we identify a regulatory subunit of skPP1M as the product of the MYPT2 gene, a protein whose sequence is 61% identical to the M110 subunit of smPP1M. Surprisingly, the M21 subunit of smPP1M appears to be produced from the same gene that encodes MYPT2. Copyright (C) 1998 Federation of European Biochemical Societies.

    KW - Muscle contraction

    KW - Myosin

    KW - Protein phosphatase 1

    UR - http://www.scopus.com/inward/record.url?scp=0031737342&partnerID=8YFLogxK

    U2 - 10.1016/S0014-5793(98)01276-9

    DO - 10.1016/S0014-5793(98)01276-9

    M3 - Article

    VL - 438

    SP - 141

    EP - 144

    JO - FEBS Letters

    JF - FEBS Letters

    SN - 0014-5793

    IS - 3

    ER -