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.