HSF1A

HSF1A is a cell-permeable activator of heat shock transcription factor 1 (HSF1)[1]. HSF1A also acts as a specific inhibitor of TRiC/CCT. Chaperonin TCP-1 ring complex (TRiC)/chaperonin containing TCP-1 (CCT) plays a pivotal role in toxin translocation and/or refolding[4].

[1]Neef DW, et al. A direct regulatory interaction between chaperonin TRiC and stress-responsive transcription factor HSF1. Cell Rep. 2014 Nov 6;9(3):955-66.|[2]Neef DW, et al. Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease. PLoS Biol. 2010 Jan 19;8(1):e1000291.|[3]Huang CY, et al. Doxorubicin attenuates CHIP-guarded HSF1 nuclear translocation and protein stability to trigger IGF-IIR-dependent cardiomyocyte death. Cell Death Dis. 2016 Nov 3;7(11):e2455.|[4]Marcus Steinemann, et al. The chaperonin TRiC/CCT is essential for the action of bacterial glycosylating protein toxins like <i>Clostridium difficile</i> toxins A and B. Proc Natl Acad Sci U S A. 2018 Sep 18;115(38):9580-9585.