Protein N-glycosylation, protein folding, and protein quality control

Jürgen Roth, Christian Zuber, Sujin Park, Insook Jang, Yangsin Lee, Katarina Gaplovska Kysela, Valérie Le Fourn, Roger Santimaria, Bruno Guhl, Jin Won Cho

Research output: Contribution to journalReview article

101 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)497-506
Number of pages10
JournalMolecules and cells
Volume30
Issue number6
DOIs
Publication statusPublished - 2010 Dec 1

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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  • Cite this

    Roth, J., Zuber, C., Park, S., Jang, I., Lee, Y., Kysela, K. G., Le Fourn, V., Santimaria, R., Guhl, B., & Cho, J. W. (2010). Protein N-glycosylation, protein folding, and protein quality control. Molecules and cells, 30(6), 497-506. https://doi.org/10.1007/s10059-010-0159-z