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Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt

Science  24 Oct 1997:
Vol. 278, Issue 5338, pp. 687-689
DOI: 10.1126/science.278.5338.687

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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.

  • * To whom correspondence should be addressed. E-mail: Gabriel.Nunez{at}umich.edu

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