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Regulation of the unfolded protein response in yeast by oxidative stress
Author(s) -
GuerraMoreno Angel,
Ang Jessie,
Welsch Hendrik,
Jochem Marco,
Hanna John
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13389
Subject(s) - unfolded protein response , oxidative stress , caenorhabditis elegans , yeast , microbiology and biotechnology , saccharomyces cerevisiae , transcription factor , biology , endoplasmic reticulum , gene , biochemistry
In the unfolded protein response ( UPR ), Ire1 activates Hac1 to coordinate the transcription of hundreds of genes to mitigate ER stress. Recent work in Caenorhabditis elegans suggests that oxidative stress inhibits this canonical Ire1 signalling pathway, activating instead an antioxidant stress response. We sought to determine whether this novel mode of UPR function also existed in yeast, where Ire1 has been best characterized. We show that the yeast UPR is also subject to inhibition by oxidative stress. Inhibition is mediated by a single evolutionarily conserved cysteine, and affects both luminal and membrane pathways of Ire1 activation. In yeast, Ire1 appears dispensable for resistance to oxidative stress and, therefore, the physiological significance of this pathway remains to be demonstrated.