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Mol. Cells 2010; 30(6): 497-506

Published online November 26, 2010

https://doi.org/10.1007/s10059-010-0159-z

© The Korean Society for Molecular and Cellular Biology

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

J?rgen Roth*, Christian Zuber1, Sujin Park, Insook Jang, Yangsin Lee, Katarina Gaplovska Kysela1,2, Val?rie Le Fourn1,3, Roger Santimaria1, Bruno Guhl1,4, and Jin Won Cho

Department of Integrated OMICs for Biomedical Sciences, WCU Program of Graduate School, Yonsei University, Seoul 120-749, Korea, 1Division of Cell and Molecular Pathology, Department of Pathology, University of Zurich, CH-8091 Zurich, Switzerland, 2Present address: Department of Genetics, Comenius University, SK-842 15 Bratislava, Slovakia, 3Present address: Selexis SA, CH-1228 Plan-les-Ouates/Geneva, Switzerland, 4Present address: Center for Microscopy and Image Analysis, University of Zurich-Irchel, CH-8057 Zurich, Switzerland

Correspondence to : *Correspondence: jurgen.roth@yonsei.ac.kr

Received: November 8, 2010; Accepted: November 11, 2010

Abstract

Quality control of protein folding represents a funda-mental 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.

Keywords electron microscopy, endoplasmic reticulum, N-glycosylation, protein folding, protein quality control

Article

Minireview

Mol. Cells 2010; 30(6): 497-506

Published online December 31, 2010 https://doi.org/10.1007/s10059-010-0159-z

Copyright © The Korean Society for Molecular and Cellular Biology.

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

J?rgen Roth*, Christian Zuber1, Sujin Park, Insook Jang, Yangsin Lee, Katarina Gaplovska Kysela1,2, Val?rie Le Fourn1,3, Roger Santimaria1, Bruno Guhl1,4, and Jin Won Cho

Department of Integrated OMICs for Biomedical Sciences, WCU Program of Graduate School, Yonsei University, Seoul 120-749, Korea, 1Division of Cell and Molecular Pathology, Department of Pathology, University of Zurich, CH-8091 Zurich, Switzerland, 2Present address: Department of Genetics, Comenius University, SK-842 15 Bratislava, Slovakia, 3Present address: Selexis SA, CH-1228 Plan-les-Ouates/Geneva, Switzerland, 4Present address: Center for Microscopy and Image Analysis, University of Zurich-Irchel, CH-8057 Zurich, Switzerland

Correspondence to:*Correspondence: jurgen.roth@yonsei.ac.kr

Received: November 8, 2010; Accepted: November 11, 2010

Abstract

Quality control of protein folding represents a funda-mental 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.

Keywords: electron microscopy, endoplasmic reticulum, N-glycosylation, protein folding, protein quality control

Mol. Cells
Jan 31, 2023 Vol.46 No.1, pp. 1~67
COVER PICTURE
RNAs form diverse shapes and play multiple functions as central molecules of gene expression. In this special issue on RNA, seven minireviews illustrate how basic concepts and recent RNA biology findings are transformed into new and exciting RNA therapeutics.

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