Journal
NATURE CELL BIOLOGY
Volume 17, Issue 7, Pages 829-838Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb3184
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Funding
- ECOS-CONICYT [C13S02]
- Ring Initiative [ACT1109]
- FONDEF [D11I1007]
- Millennium Institute [P09-015-F]
- Frick Foundation
- FONDECYT [1140549]
- Michael J. Fox Foundation for Parkinson Research
- COPEC-UC Foundation
- CONICYT [USA2013-0003]
- Institut National du Cancer (PLBio)
- Institut National du Cancer (ICGC)
- Institut National du Cancer (INCa)
- La Ligue Nationale Contre le Cancer (LARGE)
- NIH [RO1CA136577, R01-DK095306]
- American Cancer Society Research Scholar Award
- Harrington Discovery Institute Scholar-Innovator Award
- Michael J. Fox Foundation for Parkinson's Research
- Caring for Carcinoid Foundation
- American Association for Cancer Research
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Stress induced by accumulation of misfolded proteins in the endoplasmic reticulum is observed in many physiological and pathological conditions. To cope with endoplasmic reticulum stress, cells activate the unfolded protein response, a dynamic signalling network that orchestrates the recovery of homeostasis or triggers apoptosis, depending on the level of damage. Here we provide an overview of recent insights into the mechanisms that cells employ to maintain proteostasis and how the unfolded protein response determines cell fate under endoplasmic reticulum stress.
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