Journal
JOURNAL OF BIOCHEMISTRY
Volume 146, Issue 6, Pages 743-750Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvp166
Keywords
endoplasmic reticulum; phase shift; protein degradation; protein folding; quality control
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Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan [19058009, 20247026]
- Grants-in-Aid for Scientific Research [20247026, 19058009] Funding Source: KAKEN
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The accumulation of unfolded proteins in the endoplasmic reticulum (ER) under ER stress conditions activates a series of homoeostatic responses collectively termed the unfolded protein response (UPR). The UPR is unique in which the molecular mechanisms it uses to transmit signals from the ER lumen to the nucleus are completely different to those used for signalling from the plasma membrane. An ER stress signal is sensed and transmitted across the membrane by a transmembrane protein(s) in the ER. Interestingly, the number of such functional sensors/transducers, ubiquitously expressed, has increased with evolution, for example, one in Saccharomyces cerevisiae, two in Caenorhabditis elegans and Drosophila melanogaster, and three in mammals. Accordingly, mammalian cells are able to cope with ER stress in a more sophisticated manner. Here, I summarize the mechanisms and activation consequences of UPR signalling pathways in yeast, worm, fly and mammalian cells. I also discuss how they have evolved to counteract ER stress effectively.
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