Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apo
Author: ["Helen M. Beere","Beni B. Wolf","Kelvin Cain","Dick D. Mosser","Artin Mahboubi","Tomomi Kuwana","Pankaj Tailor","Richard I. Morimoto","Gerald M. Cohen","Douglas R. Green"]
Publication: Nature Cell Biology
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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.
Cite this article
Beere, H., Wolf, B., Cain, K. et al. Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat Cell Biol 2, 469–475 (2000). https://doi.org/10.1038/35019501
