Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle. Phosphorylation of site 5 by glycogen synthase kinase-5 (casein kinase-II) is a prerequisite for phosphorylation of sites 3 by glycogen synthase kinase-3

Colin Picton, James Woodgett, Brian Hemmings, Philip Cohen

    Research output: Contribution to journalArticlepeer-review

    112 Citations (Scopus)

    Abstract

    Glycogen synthase kinase-5 (casein kinase-II) phosphorylates glycogen synthase on a serine termed site 5. This residue is just C-terminal to the 3 serines phosphorylated by glycogen synthase kinase-3, which are critical for the hormonal regulation of glycogen synthase in vivo. Although phosphorylation of site 5 does not affect the catalytic activity, it is demonstrated that this modification is a prerequisite for phosphorylation by glycogen synthase kinase-3. Since site 5 is almost fully phosphorylated in vivo under all conditions, the role of glycogen synthase kinase-5 would appear to be a novel one in forming the recognition site for another protein kinase.

    Original languageEnglish
    Pages (from-to)191-196
    Number of pages6
    JournalFEBS Letters
    Volume150
    Issue number1
    DOIs
    Publication statusPublished - 13 Dec 1982

    Keywords

    • Adrenalin
    • Calmodulin
    • Casein kinase
    • Cyclic AMP
    • Glycogen synthase
    • Insulin

    Fingerprint Dive into the research topics of 'Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle. Phosphorylation of site 5 by glycogen synthase kinase-5 (casein kinase-II) is a prerequisite for phosphorylation of sites 3 by glycogen synthase kinase-3'. Together they form a unique fingerprint.

    Cite this