Dick D. Mosser

TL;DR: It is shown, using a cell-free system, that Hsp70 prevents cytochrome c/dATP-mediated caspase activation, but allows the formation of Apaf-1 oligomers, which suppresses apoptosis by directly associating with Apf-1 and blocking the assembly of a functional apoptosome.

TL;DR: The inhibition of SAPK/JNK signaling and apoptotic protease effector steps by hsp70 likely contributes to the resistance to stress-induced apoptosis seen in transiently induced thermotolerance.

TL;DR: Results reveal that the repression of heat shock gene transcription, which occurs during attenuation, is due to the association of Hsp70 with the HSF1 transactivation domain, thus providing a plausible explanation for the role of molecular chaperones in at least one key step in the autoregulation of the heat shock response.

TL;DR: The kinetics of HSP70 gene transcription paralleled the rapid appearance of stress-induced HSE-binding activity, and the DNA contacts of the control and stress- induced Hse-binding activities deduced by methylation interference were similar but not identical.

TL;DR: The results suggest that HSF is activated either directly by undergoing a conformational change or indirectly through interactions with unfolded proteins, suggesting that the transcription of heat shock genes in response to physiological stress requires activation of HSF.