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- Title
Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome.
- Authors
Beere, H M; Wolf, B B; Cain, K; Mosser, D D; Mahboubi, A; Kuwana, T; Tailor, P; Morimoto, R I; Cohen, G M; Green, D R
- Abstract
The cellular-stress response can mediate cellular protection through expression of heat-shock protein (Hsp) 70, which can interfere with the process of apoptotic cell death. Stress-induced apoptosis proceeds through a defined biochemical process that involves cytochrome c, Apaf-1 and caspase proteases. Here we show, using a cell-free system, that Hsp70 prevents cytochrome c/dATP-mediated caspase activation, but allows the formation of Apaf-1 oligomers. Hsp70 binds to Apaf-1 but not to procaspase-9, and prevents recruitment of caspases to the apoptosome complex. Hsp70 therefore suppresses apoptosis by directly associating with Apaf-1 and blocking the assembly of a functional apoptosome.
- Publication
Nature cell biology, 2000, Vol 2, Issue 8, p469
- ISSN
1465-7392
- Publication type
Journal Article
- DOI
10.1038/35019501