Heat shock induces relocalization of epigenetic modifiers to the nucleolus, which acts as a dedicated protein quality control center that is indispensable for recovery of epigenetic regulators and epigenetic modifications.
When translation stops, cells require intracellular acidification to turn on the conserved heat shock response during stress, and stress-triggered acidification (common in eukaryotes) is adaptive, promoting cell and population fitness.
Quantitative dissection of the roles of chaperone binding and phosphorylation in regulating heat shock factor 1 leads to a predictive model of the dynamics of the yeast heat shock response.
Heat-induced local unfolding allows Hsf1 to form trimers and bind to DNA, which depends on Hsf1 concentration and is promoted, not inhibited, by Hsp90.
Dynamic regulation of the heat shock response depends on a negative feedback loop in which Hsf1 activates expression of Hsp70 and Hsp70 specifically and directly represses Hsf1 transactivation.
Helitron transposable elements, by providing high density transcription factor binding sites upstream of host genes, have diversified the heat shock response within and among Caenorhabditis species.
Eukaryotic translation elongation factor 1A1 controls the process of heat shock response, from transcriptional activation of the HSP70 gene, to HSP70 mRNA stabilization, nuclear export, and translation.
A new unfolded protein response has been discovered that is distinct from the heat shock response and protects mammalian cells from proteotoxic stress.
Multiple iso-energetic-specific interactions involving the intrinsically-disordered region of sHSP HSPB1 define a quasi-ordered state, providing insights into inherited disease-associated mutations within the region that are thought to be disordered.
