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Regulation of Cell Death Protease Caspase-9 by Phosphorylation

Cardone, Michael H., Roy, Natalie, Stennicke, Henning R., Salvesen, Guy S., Franke, Thomas F., Stanbridge, Eric, Frisch, Steven, Reed, John C.·1998·Science
DOI 10.1126/science.282.5392.1318
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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.

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Research works printed but not linked: 31

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Metadata

Authors
Cardone, M. H., Roy, N., Stennicke, H. R., Salvesen, G. S., Franke, T. F., Stanbridge, E., Frisch, S., & Reed, J. C.
Affiliations
M. H. Cardone, Program on Apoptosis and Cell Death Research, The Burnham Institute, La Jolla, CA 92037, USA, and Department of Biology, Massachusetts Institute of Technology (MIT), Cambridge, MA 02139, USA. N. Roy, H. R. Stennicke, G. S. Salvesen, S. Frisch, J. C. Reed, Program on Apoptosis and Cell Death Research, The Burnham Institute, La Jolla, CA 92037, USA. T. F. Franke, Department of Pharmacology, Columbia University, New York, NY 10032, USA. E. Stanbridge, Department of Microbiology and...
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1998-11-13
Volume
282
Issue
5392
Pages
1318-1321
ISSN
  • 0036-8075
  • 1095-9203
DOI
10.1126/science.282.5392.1318
Cited by
2,481
References
0
Language
en

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