Journal
TRENDS IN CELL BIOLOGY
Volume 23, Issue 11, Pages 547-555Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2013.06.005
Keywords
unfolded protein response; ER stress; IRE1; cell fate; protein quality control; membrane trafficking system
Categories
Funding
- National Institutes of Health [R01 GM101038-01]
- Chemical Sciences, Geosciences, and Biosciences Division, Office of Basic Energy Sciences, Office of Science, U.S. DOE [DE-FG02-91ER20021]
- NASA [NNX12AN71G]
- National Science Foundation [MCB0948584, MCB1243792]
- NASA [NNX12AN71G, 69794] Funding Source: Federal RePORTER
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Cells operate a signaling network termed the unfolded protein response (UPR) to monitor protein-folding capacity in the endoplasmic reticulum (ER). Inositol-requiring enzyme 1 (IRE1) is an ER transmembrane sensor that activates the UPR to maintain the ER and cellular function. Although mammalian IRE1 promotes cell survival, it can initiate apoptosis via decay of antiapoptotic miRNAs. Convergent and divergent IRE1 characteristics between plants and animals underscore its significance in cellular homeostasis. This review provides an updated scenario of the IRE1 signaling model, discusses emerging IRE1 sensing mechanisms, compares IRE1 features among species, and outlines exciting future directions in UPR research.
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