Phosphorylation site specificities of glycogen synthase kinases: Determination by peptide mapping using high-performance liquid chromatography

Henning Juhl, Virender S. Sheorain, Charles M. Schworer, Mary Frances Jett, Thomas R. Soderling

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    20 Scopus citations


    A method is described which separates the various phosphorylation sites in glycogen synthase based on reverse phase high-performance liquid chromatography (HPLC) of tryptic 32P-peptides. Using this method we studied the phosphorylation site specificities of the kinases which act on glycogen synthase. The cAMP-dependent protein kinase phosphorylated sites 1a, 1b, and 2, whereas casein kinase II phosphorylated only site 5. Two calcium, calmodulin-dependent kinases, phosphorylase kinase and liver calmodulin-dependent synthase kinase, both phosphorylated site 2, and the latter enzyme also phosphorylated site 1b. A cAMP-independent kinase (kinase 4) purified from liver also specifically phosphorylated site 2. Synthase kinase 3 catalyzed the phosphorylation of only site 3. This HPLC method was also used to establish that all of these sites were subject to phosphorylation in vivo.

    Original languageEnglish (US)
    Pages (from-to)518-526
    Number of pages9
    JournalArchives of Biochemistry and Biophysics
    Issue number2
    StatePublished - Apr 15 1983


    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology

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