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Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9.

Authors
  • Roth, Jürgen1
  • Zuber, Christian2
  • 1 Division of Cell and Molecular Pathology, University of Zurich, 8091, Zurich, Switzerland. [email protected]
  • 2 Division of Cell and Molecular Pathology, University of Zurich, 8091, Zurich, Switzerland.
Type
Published Article
Journal
Histochemistry and cell biology
Publication Date
February 2017
Volume
147
Issue
2
Pages
269–284
Identifiers
DOI: 10.1007/s00418-016-1513-9
PMID: 27803995
Source
Medline
Keywords
License
Unknown

Abstract

Protein N-glycosylation and quality control of protein folding as well as the connected ER-associated degradation of misfolded glycoproteins (ERAD) are not only evolutionary highly conserved but also functionally linked. It is now established that particular N-glycan structures which result from processing reactions by exo-glycosidases in the ER are of importance for glycoprotein folding and for ERAD. Thus, mono-glucosylated N-glycan intermediates harbor structural information which is important for promoting glycoprotein folding. On the other hand, specific mannose-trimmed N-glycans harbor structural information for routing misfolded glycoproteins to ERAD. In this review, we summarize current knowledge concerning the role played by glucosidases I and II, in concert with the bifunctional glucosyltransferase and calnexin/calreticulin in glycoprotein folding, the role of conventional ER mannosidase I in concert with the mannosidase EDEM1 in handling and routing of misfolded glycoproteins, and how the bifunctional OS-9 provides a link to the ER dislocon for degradation.

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