The mechanism by which epidermal growth factor inhibits glycogen synthase kinase 3 in A431 cells

Y. Saito, J. R. Vandenheede, P. Cohen

    Research output: Contribution to journalArticle

    121 Citations (Scopus)

    Abstract

    Glycogen synthase kinase 3 (GSK3) was inhibited by 50% within 5 min when A431 cells were stimulated with epidermal growth factor (EGF). The inhibition was unaffected by rapamycin at concentrations which blocked the activation of p70 S6 kinase, and reversed by incubation with protein phosphatase-1. EGF stimulation of A431 cells inhibited GSK3α and GSK3β to a similar extent, and inhibition was accompanied by phosphorylation of the tryptic peptides containing the serine residues phosphorylated in vitro by p70 S6 kinase or MAP kinase-activated protein (MAPKAP) kinase-1β (also termed Rsk-2). These results demonstrate that EGF inhibits GSK3 by inducing phosphorylation of a serine residue and that GSK3 is not phosphorylated in vivo by either p70 S6 kinase or protein kinase C.

    Original languageEnglish
    Pages (from-to)27-31
    Number of pages5
    JournalBiochemical Journal
    Volume303
    Issue number1
    DOIs
    Publication statusPublished - 1 Oct 1994

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