Mechanisms of productive folding and endoplasmic reticulum-associated degradation of glycoproteins and non-glycoproteins

The quality of proteins destined for the secretory pathway is ensured by two distinct mechanisms in endoplasmic reticulum (ER): productive folding newly synthesized proteins, which assisted ER-localized molecular chaperones and most cases also disulfide bond formation transfer an oligosaccharide unit; ER-associated degradation (ERAD), unfolded or misfolded ER are recognized processed delivery to membrane complex, retrotranslocated through complex with simultaneous ubiquitination, extracted AAA-ATPase cytosol, finally degraded proteasome. We describe ERAD, particular attention glycoproteins versus non-glycoproteins, yeast mammalian systems. Molecular non-glycoproteins mediated protein isomerases well conserved from mammals. Additionally, mammals have gained structure-dependent cycle glycoproteins. ERAD mammals, but redundant expression orthologues has been encountered, particularly components involved recognition processing retrotranslocation ubiquitination non-glycoproteins. This may reflect evolutionary consequence increasing quantity needs toward introduction innovative genome editing technology into analysis as exemplified here, will provide new insights pathogenesis various diseases. • Quality control essential life. mechanism (ER) summarized. then Advances on highlighted.