A chimeric mutant analysis in yeast cells suggests BiP independent regulation of the mammalian endoplasmic reticulum-stress sensor IRE1α

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 chaper...

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Published inBioscience, biotechnology, and biochemistry Vol. 82; no. 9; pp. 1527 - 1530
Main Authors Mai, Thanh Chi, Munakata, Takeo, Tran, Duc Minh, Takagi, Hiroshi, Kimata, Yukio
Format Journal Article
LanguageEnglish
Published England Taylor & Francis 02.09.2018
Oxford University Press
Subjects
biotechnology
endoplasmic reticulum
mammals
molecular chaperone
mutants
organelle
stress response
stress sensing
transmembrane proteins
unfolded protein response
yeasts
unfolded protein response
molecular chaperone
stress response
stress sensing
organelle
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ISSN0916-8451
1347-6947
1347-6947
DOI10.1080/09168451.2018.1478716

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Summary: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.
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ISSN:0916-8451
1347-6947
1347-6947
DOI:10.1080/09168451.2018.1478716