PT - JOURNAL ARTICLE AU - Peso, Luis del AU - González-Garcı́a, Maribel AU - Page, Carmen AU - Herrera, Román AU - Nuñez, Gabriel TI - Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt AID - 10.1126/science.278.5338.687 DP - 1997 Oct 24 TA - Science PG - 687--689 VI - 278 IP - 5338 4099 - http://science.sciencemag.org/content/278/5338/687.short 4100 - http://science.sciencemag.org/content/278/5338/687.full SO - Science1997 Oct 24; 278 AB - 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.