Journal
PHARMACOLOGY & THERAPEUTICS
Volume 134, Issue 3, Pages 306-316Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.pharmthera.2012.02.003
Keywords
Apoptosis; Bcl-2 family; Endoplasmic reticulum (ER) stress; Unfolded protein response (UPR)
Categories
Funding
- Science Foundation Ireland [09/RFP/BIC2371, 09/RFP/BMT2153]
- Health Research Board [HRA/2009/59]
- Breast Cancer Campaign [2008NovPhD21, 2010NovPR13]
- Science Foundation Ireland (SFI) [09/RFP/BIC2371, 09/RFP/BMT2153] Funding Source: Science Foundation Ireland (SFI)
- Breast Cancer Campaign [2010NovPR13] Funding Source: researchfish
- Health Research Board (HRB) [HRA-2009-59] Funding Source: Health Research Board (HRB)
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available