6533b821fe1ef96bd127bac6

RESEARCH PRODUCT

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

Maria Antonietta De MatteisPiero PignataroGiuseppina AmodioPaolo RemondelliOrnella MoltedoRossella Venditti

subject

Vesicular Transport ProteinsBiophysicsEndoplasmic ReticulumBiochemistryCell LineVesicular Transport ProteinGeneticStructural BiologyERESGeneticsVesicular Transport ProteinsHumansCOPIIEndoplasmic Reticulum StreMolecular BiologyCOPIIChemistryVesicleEndoplasmic reticulumSec23Cell BiologyCOP-Coated VesiclesSEC23AEndoplasmic Reticulum StressCell biologyBiophysicUnfolded protein responseER streProtein foldingCOP-Coated VesiclesER stressCOP-Coated VesicleHumanProtein Binding

description

AbstractExit 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.

yearjournalcountryeditionlanguage
2013-01-01FEBS Letters
https://doi.org/10.1016/j.febslet.2013.08.021