Abstract
Impaired protein folding in the endoplasmic reticulum (ER) evokes the unfolded protein response (UPR), which is triggered in budding yeast, Saccharomyces cerevisiae, by the ER-located transmembrane protein Ire1. Here, we report that ethanol stress damages protein folding in the ER, causing activation of Ire1 in yeast cells. The UPR likely contributes to the ethanol tolerance of yeast cells.
Keywords:
Saccharomyces cerevisiae; endoplasmic reticulum; ethanol; stress tolerance; unfolded protein response.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Endoplasmic Reticulum Stress / drug effects*
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Enzyme Activation / drug effects
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Ethanol / pharmacology*
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Membrane Glycoproteins / metabolism*
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Protein Folding / drug effects*
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Protein Serine-Threonine Kinases / metabolism*
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Saccharomyces cerevisiae / cytology
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Saccharomyces cerevisiae / drug effects*
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / metabolism*
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Unfolded Protein Response / drug effects*
Substances
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Membrane Glycoproteins
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Saccharomyces cerevisiae Proteins
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Ethanol
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IRE1 protein, S cerevisiae
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Protein Serine-Threonine Kinases