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    Science. 1997 Oct 24;278(5338):687-9.

    Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt.

    del Peso L, González-García M, Page C, Herrera R, Nuñez G.

    Source

    Department of Pathology and Comprehensive Cancer Center, University of Michigan Medical School, Ann Arbor, MI 48109, USA.

    Abstract

    BAD is a distant member of the Bcl-2 family that promotes cell death. Phosphorylation of BAD prevents this. BAD phosphorylation induced by interleukin-3 (IL-3) was inhibited by specific inhibitors of phosphoinositide 3-kinase (PI 3-kinase). Akt, a survival-promoting serine-threonine protein kinase, was activated by IL-3 in a PI 3-kinase-dependent manner. Active, but not inactive, forms of Akt were found to phosphorylate BAD in vivo and in vitro at the same residues that are phosphorylated in response to IL-3. Thus, the proapoptotic function of BAD is regulated by the PI 3-kinase-Akt pathway.

    PMID:
    9381178
    [PubMed - indexed for MEDLINE]

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