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Detalle de: Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt

Title Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt
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.

Apa Reference Peso, L.d., González-Garcı́a, M., Page, C., Herrera, R. & Nuñez, G. (1997). Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt. Science, 278(5338), 687-689. 10.1126/science.278.5338.687
Doi 10.1126/science.278.5338.687
Publication Date 24 Oct 1997
Publication Type Article
Researcher Luis del Peso Ovalle
Ontology Drug Discovery and design
Research Groups
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