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- Title
Regulation of cell death protease caspase-9 by phosphorylation.
- Authors
Cardone, M H; Roy, N; Stennicke, H R; Salvesen, G S; Franke, T F; Stanbridge, E; Frisch, S; Reed, J C
- Abstract
Caspases are intracellular proteases that function as initiators and effectors of apoptosis. The kinase Akt and p21-Ras, an Akt activator, induced phosphorylation of pro-caspase-9 (pro-Casp9) in cells. Cytochrome c-induced proteolytic processing of pro-Casp9 was defective in cytosolic extracts from cells expressing either active Ras or Akt. Akt phosphorylated recombinant Casp9 in vitro on serine-196 and inhibited its protease activity. Mutant pro-Casp9(Ser196Ala) was resistant to Akt-mediated phosphorylation and inhibition in vitro and in cells, resulting in Akt-resistant induction of apoptosis. Thus, caspases can be directly regulated by protein phosphorylation.
- Publication
Science (New York, N.Y.), 1998, Vol 282, Issue 5392, p1318
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.282.5392.1318