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Nat Cell Biol. 2015 Jul;17(7):829-38. doi: 10.1038/ncb3184.

Proteostasis control by the unfolded protein response.

Author information

1
Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, Chile; the Institute of Biomedical Sciences (ICBM), Program of Cellular and Molecular Biology, Center for Molecular Studies of the Cell, University of Chile, Santiago, Chile; and in the Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, Massachusetts 02115, USA.
2
ER440, Oncogenesis, stress and signaling, University of Rennes 1, 35000 Rennes, France; and in the Centre Régional de Lutte Contre le Cancer Eugène Marquis, 35000 Rennes, France.
3
Department of Pathology, Diabetes Center, and Helen Diller Family Comprehensive Cancer Center, University of California, San Francisco, California 94143, USA.

Abstract

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.

PMID:
26123108
PMCID:
PMC5546321
DOI:
10.1038/ncb3184
[Indexed for MEDLINE]
Free PMC Article
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