Lipid-dependent regulation of the unfolded protein response

被引：198
作者：
Volmer, Romain [1 ,2 ,3 ,4 ]
Ron, David [1 ,2 ,3 ]
机构：
[1] Univ Cambridge, Cambridge Inst Med Res, Cambridge, England
[2] Wellcome Trust MRC Inst Metab Sci, Cambridge, England
[3] NIHR Cambridge Biomed Res Ctr, Cambridge, England
[4] Univ Toulouse, INP, ENVT, INRA,UMR 1225,IHAP, Toulouse, France
来源：
CURRENT OPINION IN CELL BIOLOGY | 2015年 / 33卷
基金：
英国惠康基金;
关键词：
ENDOPLASMIC-RETICULUM STRESS; ER STRESS; SACCHAROMYCES-CEREVISIAE; B-CELLS; TRANSMEMBRANE DOMAINS; MEMBRANE-LIPIDS; MODEL MEMBRANES; QUALITY-CONTROL; HOMEOSTASIS; ACTIVATION;
D O I：
10.1016/j.ceb.2014.12.002
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
Protein folding homeostasis in the lumen of the endoplasmic reticulum is defended by signal transduction pathways that are activated by an imbalance between unfolded proteins and chaperones (so called ER stress). Collectively referred to as the unfolded protein response (UPR) this homeostatic response is initiated by three known ER stress transducers: IRE1, PERK and ATF6. These ER-localised transmembrane (TM) proteins posses lumenal stress sensing domains and cytosolic effector domains that collectively activate a gene expression programme regulating the production of proteins involved in the processing and maturation of secreted proteins that enter the ER. However, beyond limiting unfolded protein stress in the ER the UPR has important connections to lipid metabolism that are the subject of this review.
引用
收藏
页码：67 / 73
页数：7
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