Endoplasmic Reticulum Stress Sensing in the Unfolded Protein Response
University of California, San Francisco · Howard Hughes Medical Institute
Abstract
Secretory and transmembrane proteins enter the endoplasmic reticulum (ER) as unfolded proteins and exit as either folded proteins in transit to their target organelles or as misfolded proteins targeted for degradation. The unfolded protein response (UPR) maintains the protein-folding homeostasis within the ER, ensuring that the protein-folding capacity of the ER meets the load of client proteins. Activation of the UPR depends on three ER stress sensor proteins, Ire1, PERK, and ATF6. Although the consequences of activation are well understood, how these sensors detect ER stress remains unclear. Recent evidence suggests that yeast Ire1 directly binds to unfolded proteins, which induces its oligomerization and…
Citation impact
- FWCI
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- Percentile
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- References
- 84
Authors
5- BMBrooke M. GardnerCorresponding
University of California, San Francisco
- DWDavid W. Pincus
University of California, San Francisco
- KGKatja Gotthardt
University of California, San Francisco
- CMCiara M Gallagher
University of California, San Francisco
- PWPeter Walter
Howard Hughes Medical Institute, University of California, San Francisco
Topics & keywords
- Unfolded protein response
- Endoplasmic reticulum
- ATF6
- Protein folding
- Cell biology
- Biology
- Endoplasmic-reticulum-associated protein degradation
- Transmembrane protein
Funding
- HHHoward Hughes Medical Institute
- NINational Institute for Health and Care Research
- NINational Institutes of HealthAward: 9P41GM103311
- UOUniversity of California, San Francisco
- NINational Institute of General Medical SciencesAward: 9P41GM103311
- NCNational Center for Research ResourcesAwards: 2P41RR001081, 9P41GM103311