Comparison of calmodulin-dependent glycogen synthase kinase from skeletal muscle and calmodulin-dependent protein kinase-II from brain

James R. Woodgett, Philip Cohen, Takashi Yamauchi, Hitoshi Fujisawa

    Research output: Contribution to journalArticle

    34 Citations (Scopus)

    Abstract

    Calmodulin-dependent glycogen synthase kinase from rabbit skeletal muscle and calmodulin-dependent protein kinase-II from rat brain were found to have remarkably similar substrate specificities. Both protein kinases phosphorylated synapsin-I, glycogen synthase, smooth muscle myosin light chains, histone H1 and acetyl-CoA carboxylase at the same relative rates. Site-2 of glycogen synthase was preferentially phosphorylated by both enzymes, followed by a slower phosphorylation of site-1b. Each protein kinase catalysed a 2-fold activation of tryptophan 5-monooxygenase. Calmodulin-dependent protein kinase-II and glycogen synthase kinase exhibited similar immunological cross-reactivity in the presence of Ca2+ and calmodulin, using monoclonal antibody raised against the rat brain enzyme. In the absence of Ca2+ and calmodulin, cross-reactivity of glycogen synthase kinase was decreased, whereas that of calmodulin-dependent protein kinase-II was not. The two enzymes appear to represent different isoenzymes of a multifunctional calmodulin-dependent protein kinase that may mediate many of the actions of Ca2+ in mammalian tissues. The results demonstrate that calmodulin-dependent protein kinase-II is identical to calmodulin-dependent synapsin-I kinase-II, previously shown to be very similar to calmodulin-dependent glycogen synthase kinase [(1983) FEBS Lett. 163, 329-334].

    Original languageEnglish
    Pages (from-to)49-54
    Number of pages6
    JournalFEBS Letters
    Volume170
    Issue number1
    DOIs
    Publication statusPublished - 7 May 1984

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    Glycogen Synthase Kinases
    Calcium-Calmodulin-Dependent Protein Kinase Type 2
    Calmodulin
    Muscle
    Brain
    Skeletal Muscle
    Synapsins
    Glycogen Synthase
    Protein Kinases
    Rats
    Enzymes
    Smooth Muscle Myosins
    Tryptophan Hydroxylase
    Acetyl-CoA Carboxylase
    Calcium-Calmodulin-Dependent Protein Kinases
    Myosin Light Chains
    Phosphorylation
    Substrate Specificity
    Mixed Function Oxygenases
    Tryptophan

    Keywords

    • Ca
    • Calmodulin
    • Catecholamine
    • Glycogen synthesis
    • Neurotransmitter
    • Protein phosphorylation

    Cite this

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    abstract = "Calmodulin-dependent glycogen synthase kinase from rabbit skeletal muscle and calmodulin-dependent protein kinase-II from rat brain were found to have remarkably similar substrate specificities. Both protein kinases phosphorylated synapsin-I, glycogen synthase, smooth muscle myosin light chains, histone H1 and acetyl-CoA carboxylase at the same relative rates. Site-2 of glycogen synthase was preferentially phosphorylated by both enzymes, followed by a slower phosphorylation of site-1b. Each protein kinase catalysed a 2-fold activation of tryptophan 5-monooxygenase. Calmodulin-dependent protein kinase-II and glycogen synthase kinase exhibited similar immunological cross-reactivity in the presence of Ca2+ and calmodulin, using monoclonal antibody raised against the rat brain enzyme. In the absence of Ca2+ and calmodulin, cross-reactivity of glycogen synthase kinase was decreased, whereas that of calmodulin-dependent protein kinase-II was not. The two enzymes appear to represent different isoenzymes of a multifunctional calmodulin-dependent protein kinase that may mediate many of the actions of Ca2+ in mammalian tissues. The results demonstrate that calmodulin-dependent protein kinase-II is identical to calmodulin-dependent synapsin-I kinase-II, previously shown to be very similar to calmodulin-dependent glycogen synthase kinase [(1983) FEBS Lett. 163, 329-334].",
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    Comparison of calmodulin-dependent glycogen synthase kinase from skeletal muscle and calmodulin-dependent protein kinase-II from brain. / Woodgett, James R.; Cohen, Philip; Yamauchi, Takashi; Fujisawa, Hitoshi.

    In: FEBS Letters, Vol. 170, No. 1, 07.05.1984, p. 49-54.

    Research output: Contribution to journalArticle

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