Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1

J. Ann Le Good, Wolfgang H. Ziegler, Davey B. Parekh, Dario R. Alessi, Philip Cohen, Peter J. Parker (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    955 Citations (Scopus)

    Abstract

    Phosphorylation sites in members of the protein kinase A (PKA), PKG, and PKC kinase subfamily are conserved. Thus, the PKB kinase PDK1 may be responsible for the phosphorylation of PKC isotypes. PDK1 phosphorylated the activation loop sites of PKCζ and PKCδ in vitro and in a phosphoinositide 3-kinase (PI 3-kinase)-dependent manner in vivo in human embryonic kidney (293) cells. All members of the PKC family tested formed complexes with PDK1, PDK1-dependent phosphorylation of PKCδ in vitro was stimulated by combined PKC and PDK1 activators. The activation loop phosphorylation of PKCδ in response to serum stimulation of cells was PI 3-kinase-dependent and was enhanced by PDK1 coexpression.

    Original languageEnglish
    Pages (from-to)2042-2045
    Number of pages4
    JournalScience
    Volume281
    Issue number5385
    DOIs
    Publication statusPublished - 25 Sep 1998

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