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Gorman, AM,Healy, SJM,Jager, R,Samali, A
2012
June
Stress management at the ER: Regulators of ER stress-induced apoptosis
Published
1
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Apoptosis Bcl-2 family Endoplasmic reticulum (ER) stress Unfolded protein response (UPR) ENDOPLASMIC-RETICULUM-STRESS UNFOLDED PROTEIN RESPONSE NF-KAPPA-B INDUCED CELL-DEATH TRANSCRIPTION FACTOR MAMMALIAN-CELLS CASPASE-8 ACTIVATION MEDIATED APOPTOSIS NEGATIVE REGULATOR PROAPOPTOTIC BAX
The endoplasmic reticulum (ER) is an elaborate cellular organelle essential for cell function and survival. Conditions that interfere with ER function lead to the accumulation and aggregation of unfolded proteins which are detected by ER transmembrane receptors that initiate the unfolded protein response (UPR) to restore normal ER function. If the ER stress is prolonged, or the adaptive response fails, apoptotic cell death ensues. Many studies have focused on how this failure initiates apoptosis, particularly because ER stress-induced apoptosis is implicated in the pathophysiology of several neurodegenerative and cardiovascular diseases. In this review we aim to shed light on the proteins that are not core components of the UPR signaling pathway but which can influence the course of the ER stress response by regulating the switch from the adaptive phase to apoptosis. (C) 2012 Elsevier Inc. All rights reserved.
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DOI 10.1016/j.pharmthera.2012.02.003
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