PMID:9381178
| Citation |
del Peso, L, González-García, M, Page, C, Herrera, R and Nuñez, G (1997) Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 278:687-9 |
|---|---|
| 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. |
| Links | |
| Keywords |
Androstadienes/pharmacology; Animals; Apoptosis; Carrier Proteins/metabolism; Cell Line; Chromones/pharmacology; Enzyme Activation; Enzyme Inhibitors/pharmacology; Humans; Interleukin-3/pharmacology; Mice; Morpholines/pharmacology; Phosphatidylinositol 3-Kinases/antagonists & inhibitors; Phosphatidylinositol 3-Kinases/metabolism; Phosphorylation; Phosphoserine/metabolism; Protein-Serine-Threonine Kinases/metabolism; Proto-Oncogene Proteins/metabolism; Proto-Oncogene Proteins c-akt; Proto-Oncogene Proteins c-bcl-2/metabolism; Recombinant Proteins/metabolism; Signal Transduction; bcl-Associated Death Protein; bcl-X Protein |
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