Regulatory functions of protein multisite phosphorylation

Thomas R. Soderling

    Research output: Contribution to journalReview articlepeer-review

    24 Scopus citations


    In recent years it has become apparent that an increasing number of proteins can be phosphorylated at several different sites. In this article protein multisite phosphorylation is discussed with reference to the enzymes glycogen synthase, pyruvate dehydrogenase, and phosphorylase kinase. Each of these enzymes contains three or more different phosphorylation sites on one or more subunits. Activation and inactivation of the enzymes appear to correlate quite well with phosphorylation of a few key sites on the protein. The other phosphorylation sites may influence other kinetic properties of the enzymes or regulate the rates of dephosphorylation of the key sites by the appropriate phosphatase. Thus, multisite phosphorylation may represent an important mechanism for regulating several functions of complex proteins.

    Original languageEnglish (US)
    Pages (from-to)157-179
    Number of pages23
    JournalMolecular and Cellular Endocrinology
    Issue number3
    StatePublished - Dec 1979

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Endocrinology


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