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Biochim Biophys Acta. 2013 Dec;1833(12):3507-17. doi: 10.1016/j.bbamcr.2013.07.024. Epub 2013 Aug 27.

When ER stress reaches a dead end.

Author information

1
Institute of Biomedical Sciences, Center for Molecular Studies of the Cell, Santiago, Chile; Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, Chile.

Abstract

Endoplasmic reticulum (ER) stress is a common feature of several physiological and pathological conditions affecting the function of the secretory pathway. To restore ER homeostasis, an orchestrated signaling pathway is engaged that is known as the unfolded protein response (UPR). The UPR has a primary function in stress adaptation and cell survival; however, under irreversible ER stress a switch to pro-apoptotic signaling events induces apoptosis of damaged cells. The mechanisms that initiate ER stress-dependent apoptosis are not fully understood. Several pathways have been described where we highlight the participation of the BCL-2 family of proteins and ER calcium release. In addition, recent findings also suggest that microRNAs and oxidative stress are relevant players on the transition from adaptive to cell death programs. Here we provide a global and integrated overview of the signaling networks that may determine the elimination of a cell under chronic ER stress. This article is part of a Special Section entitled: Cell Death Pathways.

KEYWORDS:

Adaptation; Apoptosis; Cell death; ER stress; Unfolded protein response

PMID:
23988738
DOI:
10.1016/j.bbamcr.2013.07.024
[Indexed for MEDLINE]
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