In the present study, we find that the main regulatory response upon heat shock occurs at the TR level, although this is modulated by adjusting the mRNA stability of specific sets of genes.
In Arabidopsis, HsfA1a, HsfA1b, and HsfA1d act as the main positive regulators of heat shock response [ 20].
One typical response to heat stress is an accelerated transcription of a set of stress or protein fate-related genes, such as those encoding HSPs, which are the main constituents of the heat shock response [ 1].
Moreover, the conserved HrcA, HspR and ClgR proteins were included in this functional category since they represent main components of the heat shock response of C. glutamicum [ 32, 33].
HSP 27 and 70, two main players in the heat shock response, block apoptosis also at a post-mitochondrial level, by interacting with cytochrome c and with the other released cofactor AIF in the cytosol [5,39].
Second, heat shock proteins (main actors of the HSR) play crucial role in many fundamental cellular processes.
The CMA process, responsible for the selective degradation of aberrant proteins containing the consensus peptide sequence KFERQ, requires the presence of two main proteins: cytosolic and lysosomal heat shock cognate protein 70 (hsc70) and lysosomal-associated membrane protein 2A (lamp2A).
Protection against proteotoxicity involves four main stress response pathways: the heat shock response (HSR) (3), the unfolded protein response in the endoplasmic reticulum (UPRER) (4), the unfolded protein response in the mitochondria (UPRmt) (5) and the oxidative stress response (OxSR) (6).
TNF receptor-associated protein 1 (theP1), the main mitochondrial member of the heat shock protein (HSP) 90 family, is induced in most tumor types and is involved in the regulation of proteostasis in the mitochondria of tumor cells through the control of folding and stability of selective proteins, such as Cyclophilin D and Sorcin.
