Abstract
An endoplasmic reticulum (ER)-located transmembrane protein, Ire1, triggers cytoprotective events upon ER stress. Chimeric yeast Ire1 carrying the luminal domain of the mammalian major Ire1 paralogue IRE1α is upregulated in ER-stressed yeast cells, but is poorly associated with the ER-located chaperone BiP even under non-stressed conditions. This observation contradicts the theory that BiP is the master regulator of IRE1α.
Keywords:
molecular chaperone; organelle; stress response; stress sensing; unfolded protein response.
MeSH terms
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Basic-Leucine Zipper Transcription Factors / genetics
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Endoplasmic Reticulum Stress*
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Endoribonucleases / metabolism*
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Fungal Proteins / genetics*
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Green Fluorescent Proteins / genetics
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HSP70 Heat-Shock Proteins / genetics*
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Humans
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Microscopy, Fluorescence
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Mutant Chimeric Proteins / genetics*
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Mutation*
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Plasmids
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Protein Serine-Threonine Kinases / metabolism*
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RNA Splicing
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RNA, Messenger / genetics
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Repressor Proteins / genetics
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Reverse Transcriptase Polymerase Chain Reaction
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae Proteins / genetics
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Unfolded Protein Response
Substances
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Basic-Leucine Zipper Transcription Factors
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Fungal Proteins
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HAC1 protein, S cerevisiae
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HSP70 Heat-Shock Proteins
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KAR2 protein, yeast
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Mutant Chimeric Proteins
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RNA, Messenger
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Repressor Proteins
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Saccharomyces cerevisiae Proteins
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Green Fluorescent Proteins
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ERN1 protein, human
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Protein Serine-Threonine Kinases
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Endoribonucleases