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Endoplasmic Reticulum stress reduces COPII vesicle formation and modifies Sec23a cycling at ERESs
Author(s) -
Amodio Giuseppina,
Venditti Rossella,
De Matteis Maria Antonietta,
Moltedo Ornella,
Pignataro Piero,
Remondelli Paolo
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.08.021
Subject(s) - copii , endoplasmic reticulum , unfolded protein response , microbiology and biotechnology , vesicle , copi , secretory protein , chemistry , secretion , secretory pathway , biology , membrane , biochemistry , golgi apparatus
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.