The role of phosphorylase kinase in the nervous and hormonal control of glycogenolysis in muscle

    Research output: Contribution to journalReview article

    38 Citations (Scopus)

    Abstract

    The total dependence of phosphorylase kinase activity on calcium ions synchronizes glycogenolysis with the onset of muscle contraction. The activity is also stimulated by phosphorylation of the enzyme, a reaction catalysed by cyclic AMP dependent protein kinase and also by phosphorylase itself. Phosphorylase kinase possesses the structure (αβγ) 4, where the mol wts of the three protein subunits α, β and γ are 145,000, 130,000 and 45,000 respectively. The 40 fold activation produced by cyclic AMP dependent protein kinase is paralleled by the phosphorylation at a single site on the β subunit, although one site on the α subunit is also phosphorylated at 5 fold slower rate, without affecting the total activity. The phosphorylation of the α subunit does, however, greatly stimulate the dephosphorylation of the β subunit and inactivation of the enzyme by phosphorylase kinase phosphatase kinase may also be activated up to 100 fold by limited proteolysis, but in contrast with activation by phosphorylation this appears to correlate with a modification of the α sununit. Models for the interrelationship between the various activating mechanisms are considered, and the roles of the three sununits are discussed in terms of electron micrographs of the enzyme molecule.

    Original languageEnglish
    Pages (from-to)51-73
    Number of pages23
    JournalBiochemical Society Symposia
    VolumeVol. 39
    Publication statusPublished - 1 Dec 1974

    Fingerprint

    Phosphorylase Kinase
    Glycogenolysis
    Phosphorylation
    Muscle
    Muscles
    Cyclic AMP-Dependent Protein Kinases
    Enzymes
    Chemical activation
    Proteolysis
    Phosphorylases
    Protein Subunits
    Muscle Contraction
    Phosphotransferases
    Electrons
    Ions
    Calcium
    Molecules

    Cite this

    @article{fec0c81b8e644c78b392efc61a856d7c,
    title = "The role of phosphorylase kinase in the nervous and hormonal control of glycogenolysis in muscle",
    abstract = "The total dependence of phosphorylase kinase activity on calcium ions synchronizes glycogenolysis with the onset of muscle contraction. The activity is also stimulated by phosphorylation of the enzyme, a reaction catalysed by cyclic AMP dependent protein kinase and also by phosphorylase itself. Phosphorylase kinase possesses the structure (αβγ) 4, where the mol wts of the three protein subunits α, β and γ are 145,000, 130,000 and 45,000 respectively. The 40 fold activation produced by cyclic AMP dependent protein kinase is paralleled by the phosphorylation at a single site on the β subunit, although one site on the α subunit is also phosphorylated at 5 fold slower rate, without affecting the total activity. The phosphorylation of the α subunit does, however, greatly stimulate the dephosphorylation of the β subunit and inactivation of the enzyme by phosphorylase kinase phosphatase kinase may also be activated up to 100 fold by limited proteolysis, but in contrast with activation by phosphorylation this appears to correlate with a modification of the α sununit. Models for the interrelationship between the various activating mechanisms are considered, and the roles of the three sununits are discussed in terms of electron micrographs of the enzyme molecule.",
    author = "P. Cohen",
    year = "1974",
    month = "12",
    day = "1",
    language = "English",
    volume = "Vol. 39",
    pages = "51--73",
    journal = "Biochemical Society Symposium",
    issn = "0067-8694",
    publisher = "Portland Press",

    }

    The role of phosphorylase kinase in the nervous and hormonal control of glycogenolysis in muscle. / Cohen, P.

    In: Biochemical Society Symposia, Vol. Vol. 39, 01.12.1974, p. 51-73.

    Research output: Contribution to journalReview article

    TY - JOUR

    T1 - The role of phosphorylase kinase in the nervous and hormonal control of glycogenolysis in muscle

    AU - Cohen, P.

    PY - 1974/12/1

    Y1 - 1974/12/1

    N2 - The total dependence of phosphorylase kinase activity on calcium ions synchronizes glycogenolysis with the onset of muscle contraction. The activity is also stimulated by phosphorylation of the enzyme, a reaction catalysed by cyclic AMP dependent protein kinase and also by phosphorylase itself. Phosphorylase kinase possesses the structure (αβγ) 4, where the mol wts of the three protein subunits α, β and γ are 145,000, 130,000 and 45,000 respectively. The 40 fold activation produced by cyclic AMP dependent protein kinase is paralleled by the phosphorylation at a single site on the β subunit, although one site on the α subunit is also phosphorylated at 5 fold slower rate, without affecting the total activity. The phosphorylation of the α subunit does, however, greatly stimulate the dephosphorylation of the β subunit and inactivation of the enzyme by phosphorylase kinase phosphatase kinase may also be activated up to 100 fold by limited proteolysis, but in contrast with activation by phosphorylation this appears to correlate with a modification of the α sununit. Models for the interrelationship between the various activating mechanisms are considered, and the roles of the three sununits are discussed in terms of electron micrographs of the enzyme molecule.

    AB - The total dependence of phosphorylase kinase activity on calcium ions synchronizes glycogenolysis with the onset of muscle contraction. The activity is also stimulated by phosphorylation of the enzyme, a reaction catalysed by cyclic AMP dependent protein kinase and also by phosphorylase itself. Phosphorylase kinase possesses the structure (αβγ) 4, where the mol wts of the three protein subunits α, β and γ are 145,000, 130,000 and 45,000 respectively. The 40 fold activation produced by cyclic AMP dependent protein kinase is paralleled by the phosphorylation at a single site on the β subunit, although one site on the α subunit is also phosphorylated at 5 fold slower rate, without affecting the total activity. The phosphorylation of the α subunit does, however, greatly stimulate the dephosphorylation of the β subunit and inactivation of the enzyme by phosphorylase kinase phosphatase kinase may also be activated up to 100 fold by limited proteolysis, but in contrast with activation by phosphorylation this appears to correlate with a modification of the α sununit. Models for the interrelationship between the various activating mechanisms are considered, and the roles of the three sununits are discussed in terms of electron micrographs of the enzyme molecule.

    UR - http://www.scopus.com/inward/record.url?scp=0016301674&partnerID=8YFLogxK

    M3 - Review article

    VL - Vol. 39

    SP - 51

    EP - 73

    JO - Biochemical Society Symposium

    JF - Biochemical Society Symposium

    SN - 0067-8694

    ER -