Regulation of the unfolded protein response in yeast by oxidative stress.
FEBS Lett
; 593(10): 1080-1088, 2019 05.
Article
em En
| MEDLINE
| ID: mdl-31002390
ABSTRACT
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
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Glicoproteínas de Membrana
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Regulação Fúngica da Expressão Gênica
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Proteínas Serina-Treonina Quinases
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Estresse Oxidativo
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Proteínas de Saccharomyces cerevisiae
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Resposta a Proteínas não Dobradas
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article