Quality control in the endoplasmic reticulum protein factory

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Cell death in the nervous system (2006, background): “Although this response may put off a cellular catastrophe for a short time, prolonged ER stress and UPR activation completely overwhelm the cellular protective mechanism, ultimately resulting in the activation of suicide pathway”
ER stress (PERK/eIF2α phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation (2007, background): “unfolded or malfolded proteins in the ER are retrotranslocated to the cytoplasm and degraded by the ER-associated ubiquitine/proteasome degradation (ERAD) system.(15) How-”
Signal integration in the endoplasmic reticulum unfolded protein response (2007, background): “The UPR directly regulates the expression of the chaperones and degradation machinery that constitute the ER quality control system that retains attempts to fold but, ultimately, destroys most such mutant protein”
Protein quality control in the early secretory pathway (2008, background): “Protein QC (Box 1) is intimately linked to the processes of folding (Ellgaard and Helenius, 2003; Sitia and Braakman, 2003).”