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Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9.
- Source :
-
Histochemistry & Cell Biology . Feb2017, Vol. 147 Issue 2, p269-284. 16p. - Publication Year :
- 2017
-
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. [ABSTRACT FROM AUTHOR]
- Subjects :
- *GLYCOPROTEINS
*PROTEIN folding
*GLYCANS
*ENDOPLASMIC reticulum
*PROTEOLYSIS
Subjects
Details
- Language :
- English
- ISSN :
- 09486143
- Volume :
- 147
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Histochemistry & Cell Biology
- Publication Type :
- Academic Journal
- Accession number :
- 121186053
- Full Text :
- https://doi.org/10.1007/s00418-016-1513-9