Phosphorylation of K-casein by glycogen synthase kinase-3 from rabbit skeletal muscle

Arianna Donella-Deana, Lorenza A. Pinna, Brian Hemmings, Philip Cohen

    Research output: Contribution to journalArticlepeer-review

    2 Citations (Scopus)

    Abstract

    Glycogen synthase kinase-3 (ATP: protein phosphotransferase, EC 2.7.1.37) phosphorylated K-casein 20-fold more rapidly than β-casein, while αS1-casein was not a substrate. This distinguished it from casein kinase-I and casein kinase-II, which phosphorylate the β-casein variant preferentially. Glycogen synthase kinase-3 phosphorylated a serine residue(s) in the C-terminal cyanogen bromide fragment on K-casein. In contrast, cyclic AMP-dependent protein kinase phosporylated the N-terminal fragment, and phosphorylase kinase the N-terminal and intermediate cyanogen bromide fragments. The results emphasize the potential value of casein phosphorylation as a means of classifying protein kinases.

    Original languageEnglish
    Pages (from-to)149-153
    Number of pages5
    JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
    Volume745
    Issue number2
    DOIs
    Publication statusPublished - 15 Jun 1983

    Keywords

    • (Rabbit skeletal muscle)
    • Casein kinase
    • Glycogen synthase kinase
    • Protein kinase

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