Endoplasmic Reticulum stress reduces COPII vesicle formation and modifies Sec23a cycling at ERESs

被引：27

作者：

Amodio, Giuseppina ^{[2
]}

Venditti, Rossella ^{[3
]}

De Matteis, Maria Antonietta ^{[3
]}

Moltedo, Ornella ^{[2
]}

Pignataro, Piero ^{[2
]}

Remondelli, Paolo ^{[1
]}

机构：

[1] Univ Salerno, Dipartimento Med & Chirurg, I-84081 Salerno, Italy

[2] Univ Salerno, Dipartimento Farm, I-84084 Salerno, Italy

[3] Telethon Inst Genet & Med, I-80131 Naples, Italy

来源：

FEBS LETTERS | 2013年 / 587卷 / 19期

关键词：

COPII; Sec23; ERES; ER stress; ER-EXIT SITES; UNFOLDED PROTEIN RESPONSE; GOLGI-COMPLEX; COAT PROTEINS; TRANSPORT; ORGANIZATION; MEMBRANE; SEC16; BINDING; ERGIC-53;

D O I：

10.1016/j.febslet.2013.08.021

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Exit from the Endoplasmic Reticulum (ER) of newly synthesized proteins is mediated by COPII vesicles that bud from the ER at the ER Exit Sites (ERESs). Disruption of ER homeostasis causes accumulation of unfolded and misfolded proteins in the ER. This condition is referred to as ER stress. Previously, we demonstrated that ER stress rapidly impairs the formation of COPII vesicles. Here, we show that membrane association of COPII components, and in particular of Sec23a, is impaired by ER stress-inducing agents suggesting the existence of a dynamic interplay between protein folding and COPII assembly at the ER. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：3261 / 3266

页数：6

共 41 条

[31] p125 is localized in endoplasmic reticulum exit sites and involved in their organization [J].