Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt
- 24 October 1997
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 278 (5338) , 687-689
- https://doi.org/10.1126/science.278.5338.687
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
This publication has 21 references indexed in Scilit:
- Programmed Cell Death in Animal DevelopmentCell, 1997
- Direct Regulation of the Akt Proto-Oncogene Product by Phosphatidylinositol-3,4-bisphosphateScience, 1997
- Life, death, and the pursuit of apoptosis.Genes & Development, 1996
- Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase BNature, 1995
- Molecular alterations of the AKT2 oncogene in ovarian and breast carcinomasInternational Journal of Cancer, 1995
- Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transductionNature, 1995
- Requirement for Phosphatidylinositol-3 Kinase in the Prevention of Apoptosis by Nerve Growth FactorScience, 1995
- Bad, a heterodimeric partner for Bcl-xL and Bcl-2, displaces bax and promotes cell deathCell, 1995
- Programmed Cell Death and the Control of Cell Survival: Lessons from the Nervous SystemScience, 1993
- Social controls on cell survival and cell deathNature, 1992