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.

Keywords

Protein kinase BPhosphorylationKinaseCell biologyMAP kinase kinase kinaseMAP2K7Protein kinase AMitogen-activated protein kinase kinaseChemistryCyclin-dependent kinase 2Cancer researchBiology

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Year
1997
Type
article
Volume
278
Issue
5338
Pages
687-689
Citations
2218
Access
Closed

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Luis del Peso, Maribel González-Garcı́a, Carmen Page et al. (1997). Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt. Science , 278 (5338) , 687-689. https://doi.org/10.1126/science.278.5338.687

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DOI
10.1126/science.278.5338.687