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Histochemistry and Cell Biology

, Volume 147, Issue 2, pp 269–284 | Cite as

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

  • Jürgen Roth
  • Christian Zuber
Review

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.

Keywords

Protein N-glycosylation Endoplasmic reticulum Glucosidase I Glucosidase II Glucosyltransferase ER mannosidase I EDEM1 OS-9 Protein folding ERAD 

Notes

Acknowledgements

We thank D. J. Taatjes for comments on the manuscript, and we apologize to those colleagues whose publications could not be included in this review due to space limitations. Our original work was supported by the Swiss National Science Foundation.

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© Springer-Verlag Berlin Heidelberg 2016

Authors and Affiliations

  1. 1.Division of Cell and Molecular PathologyUniversity of ZurichZurichSwitzerland

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