期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
卷 1813, 期 4, 页码 564-574出版社
ELSEVIER
DOI: 10.1016/j.bbamcr.2010.11.012
关键词
Endoplasmic reticulum; Unfolded protein response; BCL-2 family
资金
- FONDECYT [1100176, 3100033]
- FONDAP [15010006]
- Millennium Nucleus [P07-048-F, P07-011-F]
- Alzheimer's Association
- High Q Foundation-CHDI
- Michael J. Fox Foundation for Parkinson's Research
- ICGEB
- CONICYT [24090143]
The assembling of distinct signaling protein complexes at the endoplasmic reticulum (ER) membrane controls several stress responses related to calcium homeostasis. autophagy, ER morphogenesis and protein folding. Diverse pathological conditions interfere with the function of the ER altering protein folding, a condition known as ER stress. Adaptation to ER stress depends on the activation of the unfolded protein response (UPR) and protein degradation pathways such as autophagy. Under chronic or irreversible ER stress, cells undergo apoptosis, where the BCL-2 protein family plays a crucial role at the mitochondria to trigger cytochrome c release and apoptosome assembly. Several BCL2 family members also regulate physiological processes at the ER through dynamic interactomes. Here we provide a comprehensive view of the roles of the BCL-2 family of proteins in mediating the molecular crosstalk between the ER and mitochondria to initiate apoptosis, in addition to their emerging functions in adaptation to stress, including autophagy, UPR, calcium homeostasis and organelle morphogenesis. We envision a model where BCL-2-containing complexes may operate as stress rheostats that, beyond their known apoptosis functions at the mitochondria, determine the amplitude and kinetics of adaptive responses against ER-related injuries. This article is part of a Special Issue entitled Mitochondria: the deadly organelle. (C) 2010 Elsevier B.V. All rights reserved.
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