title: Protein N-glycosylation, protein folding, and protein quality control.
abstract: 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.
authors.affiliation: Department of Integrated OMICs for Biomedical Sciences, WCU Program of Graduate School, Yonsei University, Seoul 120-749, Korea. jurgen.roth@yonsei.ac.kr
authors.forename: Jürgen
authors.initials: J
authors.lastname: Roth
authors.forename: Christian
authors.initials: C
authors.lastname: Zuber
authors.forename: Sujin
authors.initials: S
authors.lastname: Park
authors.forename: Insook
authors.initials: I
authors.lastname: Jang
authors.forename: Yangsin
authors.initials: Y
authors.lastname: Lee
authors.forename: Katarina Gaplovska
authors.initials: KG
authors.lastname: Kysela
authors.forename: Valérie
authors.initials: V
authors.lastname: Le Fourn
authors.forename: Roger
authors.initials: R
authors.lastname: Santimaria
authors.forename: Bruno
authors.initials: B
authors.lastname: Guhl
authors.forename: Jin Won
authors.initials: JW
authors.lastname: Cho
mesh_terms: D004721:Endoplasmic Reticulum / Q000378:metabolism / Q000502:physiology*; D006023:Glycoproteins / Q000378:metabolism / Q000502:physiology; D006031:Glycosylation; D008358:Mannose / Q000378:metabolism; D009844:Oligosaccharides / Q000096:biosynthesis / Q000378:metabolism; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D000520:alpha-Glucosidases / Q000378:metabolism
chemical_list: D006023:Glycoproteins; D009844:Oligosaccharides; D011506:Proteins; C034251:4-nitrophenyl-alpha-glucosidase; C042059:glucosidase I; D000520:alpha-Glucosidases; D008358:Mannose