Protein N-Glycosylation, Protein Folding, and Protein Quality Control

• Published in: Molecules and cells 2010, Vol.30 (6), p.497-506
• Main Authors: Roth, Jurgen, Zuber, Christian, Park, Su-Jin, Jang, In-Sook, Lee, Yang-Sin, Kysela, Katarina Gaplovska, Le Fourn, Valerie, Santimaria, Roger, Guhl, Bruno, Cho, Jin-Won
• Format: Article
• Language: Korean
• ISSN: 1016-8478; 0219-1032

Quality control of protein folding represents a fundamental cellular activity. Early steps of protein N-glycosylation involving the removal of three glucose and some specific mannose residues in the endoplasmic reticulum have been recognized as being of importance for protein quality control. Specific oligosaccharide structures resulting from the oligosaccharide processing may represent a glycocode promoting productive protein folding, whereas others may represent glyco-codes for routing not correctly folded proteins for dislocation from the endoplasmic reticulum to the cytosol and subsequent degradation. Although quality control of protein folding is essential for the proper functioning of cells, it is also the basis for protein folding disorders since the recognition and elimination of non-native conformers can result either in loss-of-function or pathological-gain-of-function. The machinery for protein folding control represents a prime example of an intricate interactome present in a single organelle, the endoplasmic reticulum. Here, current views of mechanisms for the recognition and retention leading to productive protein folding or the eventual elimination of misfolded glycoproteins in yeast and mammalian cells are reviewed.