Substrate specificity of liver calmodulin-dependent glycogen synthase kinase

Charles M. Schworer, Thomas R. Soderling

    Research output: Contribution to journalArticle

    22 Scopus citations

    Abstract

    A number of proteins were tested as potential substrates for purified rabbit liver calmodulin-dependent glycogen synthase kinase. It was found that liver phenylalanine hydroxylase and several brain proteins including tyrosine hydroxylase, microtubule-associated protein 2, and synapsin I were readily phosphorylated. Brain tubulin was very poorly phosphorylated. These results suggest that calmodulin-dependent glycogen synthase kinase may be a more general protein kinase involved in the regulation of several cellular Ca2+-dependent functions.

    Original languageEnglish (US)
    Pages (from-to)412-416
    Number of pages5
    JournalBiochemical and Biophysical Research Communications
    Volume116
    Issue number2
    DOIs
    StatePublished - Oct 31 1983

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

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