Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome

By H. Beere, B. Wolf, K. Cain, D. Mosser, A. Mahboubi, T. Kuwana, P. Tailor, Richard I. Morimoto, G. Cohen, Douglas R. Green. Nature Cell Biology, 2000

1,570 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/bcce26b31bd5207de100035cb4df77fe63e9870c

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Citations in the corpus

The physiology and pathophysiology of nitric oxide in the brain. (2005, background): “HSP70 inhibits Apaf-1 oligomerization by binding to the Apaf-1 caspase domain (CARD), which prevents the formation of the apoptosome (Beere et al., 2000).”
`The stress of dying': the role of heat shock proteins in the regulation of apoptosis (2004, background): “…regulatory point for the anti-apoptotic effects of several Hsps. Hsp70 can inhibit the formation of a functionally competent apoptosome by directly associating with Apaf-1 to prevent the recruitment and activation of the initiator caspase pro-caspase-9 (Beere et al., 2000; Saleh et al., 2000).”
Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones. (2003, background): “Arrows, pharynx. ways influencing cell growth and death (Beere et al., 2000; Song et al., 2001; Nollen and Morimoto, 2002).”
Apoptosis and melanoma chemoresistance (2003, background): “On the other hand, Hsp70 may also interfere with classical mitochondrial cell death pathways by preventing the oligomerization of Apaf-1 (Saleh et al., 2000) and/or by blocking the recruitment of casp9 to the apoptosome (Beere et al., 2000).”
Live microbial feed supplement in aquaculture for improvement of stress tolerance (2006, background): “1990; Beere et al. 2000; Saleh et al. 2000; Ravagnan et al. 2001).”
Impact of Protein Kinase PKR in Cell Biology: from Antiviral to Antiproliferative Action (2006, background): “Hsp70 is an antiapoptotic chaperone protein (251) that inhibits mitochondrial release of cytochrome c and blocks procaspase 9 recruitment to the apoptosome complex (16).”
Mitochondria and cell death: outer membrane permeabilization and beyond (2010, background): “Various proteins, including heat shock proteins such as HSP70 and HSP90, have been shown to negatively influence apoptosome function, either by inhibiting its formation or by preventing the recruitment of pro-caspase 9 (Ref”
The Chaperone Function of hsp70 Is Required for Protection against Stress-Induced Apoptosis (2000, methodology): “In vitro experiments, using mitochondrion-free cytoplasmic extracts, revealed that purified recombinant hsp70 can inhibit cytochrome c-dATP-mediated caspase activation ( 1 , 29).”
Chaperoning signaling pathways: molecular chaperones as stress-sensing 'heat shock' proteins. (2002, background): “In addition to components of the Ras/Raf-1 signaling pathway and hormone receptors, a wide variety of other molecules interact with Hsp70 and Hsp90 chaperone complexes, including the heat shock transcription factor, Apaf1, CFTR and Hepatitis B viral reverse transcriptase (Abravaya t al., 1992; Beere”
Cellular Stress Responses: Cell Survival and Cell Death (2010, background): “In the cytosol, these Hsps can block apoptosome formation and activation of downstream caspases through their ability to bind to cytochrome c and procaspase-3 (in the case of Hsp27) [107, 108] and procaspases -3, -7 and Apaf1 (in the case of Hsp70) [101, 113–115].”