| | |  | | | | Record from Web of Science® | | | | | | |
| Regulation of cell death protease caspase-9 by phosphorylation |
|
|
| Author(s): Cardone MH, Roy N, Stennicke HR, Salvesen GS, Franke TF, Stanbridge E, Frisch S, Reed JC |
| Source: SCIENCE Volume: 282 Issue: 5392 Pages: 1318-1321 Published: NOV 13 1998 |
| Times Cited: 1,800 References: 34 |
| 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. |
| Document Type: Article |
| Language: English |
| Reprint Address: Reed, JC (reprint author), Burnham Inst, Program Apoptosis & Cell Death Res, 10901 N Torrey Pines Rd, La Jolla, CA 92037 USA |
Addresses:
1. Burnham Inst, Program Apoptosis & Cell Death Res, La Jolla, CA 92037 USA
2. MIT, Dept Biol, Cambridge, MA 02139 USA
3. Columbia Univ, Dept Pharmacol, New York, NY 10032 USA
4. Univ Calif Irvine, Dept Microbiol & Mol Genet, Irvine, CA 92697 USA |
| Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: 138PV |
| ISSN: 0036-8075 |
|
| | | | | | | | | Record from Web of Science® | | | | | | | | | |