Abstract
Endoplasmic reticulum (ER)-located protein Ire1 triggers the unfolded protein response against ER-stressing stimuli, which are categorized as ER accumulation of unfolded proteins or membrane lipid-related aberrancy. Here we demonstrate that by using yeast Ire1 mutants, we can distinguish the category to which a stress-inducing stimulus belongs. For instance, ethanol was found to activate Ire1 through both types of cellular damage.
Keywords:
Endoplasmic reticulum; UPR; membrane lipid; stress response; yeast.
MeSH terms
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Basic-Leucine Zipper Transcription Factors / genetics
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Basic-Leucine Zipper Transcription Factors / metabolism
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Endoplasmic Reticulum Stress*
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Lipid Metabolism*
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Membrane Glycoproteins / genetics
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Membrane Glycoproteins / metabolism*
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Membrane Lipids / metabolism*
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Mutation*
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism*
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Proteins / metabolism*
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RNA, Messenger / genetics
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Repressor Proteins / genetics
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Repressor Proteins / metabolism
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Unfolded Protein Response*
Substances
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Basic-Leucine Zipper Transcription Factors
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HAC1 protein, S cerevisiae
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Membrane Glycoproteins
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Membrane Lipids
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Proteins
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RNA, Messenger
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Repressor Proteins
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Saccharomyces cerevisiae Proteins
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IRE1 protein, S cerevisiae
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Protein Serine-Threonine Kinases