ER stress-induced clearance of misfolded GPI-anchored proteins via the secretory pathway.

ABSTRACT: Proteins destined for the cell surface are first assessed in the endoplasmic reticulum (ER) for proper folding before release into the secretory pathway. This ensures that defective proteins are normally prevented from entering the extracellular environment, where they could be disruptive. Here, we report that, when ER folding capacity is saturated during stress, misfolded glycosylphosphatidylinositol-anchored proteins dissociate from resident ER chaperones, engage export receptors, and quantitatively leave the ER via vesicular transport to the Golgi. Clearance from the ER commences within minutes of acute ER stress, before the transcriptional component of the unfolded protein response is activated. These aberrant proteins then access the cell surface transiently before destruction in lyso

SUBMITTER: Satpute-Krishnan P 

PROVIDER: S-EPMC4121523 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature