Open AccessManagement of the endoplasmic reticulum stress by activation of the heat shock response in yeast
Author(s) -
Hou Jin,
Tang Hongting,
Liu Zihe,
Österlund Tobias,
Nielsen Jens,
Petranovic Dina
Publication year - 2014
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/1567-1364.12125
Subject(s) - unfolded protein response , endoplasmic reticulum , biology , microbiology and biotechnology , saccharomyces cerevisiae , heat shock , hsf1 , proteostasis , heat shock protein , psychological repression , proteasome , hsp90 , cellular stress response , transcription factor , chaperone (clinical) , yeast , hsp70 , gene expression , biochemistry , gene , fight or flight response , medicine , pathology
In yeast S accharomyces cerevisiae , accumulation of misfolded proteins in the endoplasmic reticulum ( ER ) causes ER stress and activates the unfolded protein response ( UPR ), which is mediated by H ac1p. The heat shock response ( HSR ) mediated by H sf1p, mainly regulates cytosolic processes and protects the cell from stresses. Here, we find that a constitutive activation of the HSR could increase ER stress resistance in both wild‐type and UPR ‐deficient cells. Activation of HSR decreased UPR activation in the WT (as shown by the decreased HAC 1 m RNA splicing). We analyzed the genome‐wide transcriptional response in order to propose regulatory mechanisms that govern the interplay between UPR and HSR and followed up for the hypotheses by experiments in vivo and in vitro . Interestingly, we found that the regulation of ER stress response via HSR is (1) only partially dependent on over‐expression of K ar2p ( ER resident chaperone induced by ER stress); (2) does not involve the increase in protein turnover via the proteasome activity; (3) is related to the oxidative stress response. From the transcription data, we also propose that HSR enhances ER stress resistance mainly through facilitation of protein folding and secretion. We also find that HSR coordinates multiple stress–response pathways, including the repression of the overall transcription and translation.