Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
- PMID: 7736594
- DOI: 10.1016/0092-8674(95)90395-x
Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
Abstract
To determine the role of N-linked oligosaccharides in the folding of glycoproteins, we analyzed the processing of in vitro translated influenza hemagglutinin (HA) in dog pancreas microsomes. We found that binding to calnexin, a membrane-bound molecular chaperone, was specific to molecules that possessed monoglucosylated core glycans. In the microsomes, these were generated either by glucose removal from the original triglucosylated core oligosaccharide by glucosidases I and II or by reglucosylation of already unglucosylated high mannose glycans. Release of fully folded HA from calnexin required the removal of the remaining glucose by glucosidase II. The results provided an explanation for trimming and reglucosylation activities in the endoplasmic reticulum and established a direct correlation between glycosylation and folding.
Similar articles
-
Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control.Proc Natl Acad Sci U S A. 1994 Feb 1;91(3):913-7. doi: 10.1073/pnas.91.3.913. Proc Natl Acad Sci U S A. 1994. PMID: 8302866 Free PMC article.
-
Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins.Mol Biol Cell. 1995 Sep;6(9):1173-84. doi: 10.1091/mbc.6.9.1173. Mol Biol Cell. 1995. PMID: 8534914 Free PMC article.
-
The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin.J Cell Biol. 1997 Nov 3;139(3):613-23. doi: 10.1083/jcb.139.3.613. J Cell Biol. 1997. PMID: 9348279 Free PMC article.
-
Protein glucosylation and its role in protein folding.Annu Rev Biochem. 2000;69:69-93. doi: 10.1146/annurev.biochem.69.1.69. Annu Rev Biochem. 2000. PMID: 10966453 Review.
-
Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation.Biochem J. 2000 May 15;348 Pt 1(Pt 1):1-13. Biochem J. 2000. PMID: 10794707 Free PMC article. Review.
Cited by
-
Intramembrane client recognition potentiates the chaperone functions of calnexin.EMBO J. 2022 Dec 15;41(24):e110959. doi: 10.15252/embj.2022110959. Epub 2022 Oct 31. EMBO J. 2022. PMID: 36314723 Free PMC article.
-
Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9.Histochem Cell Biol. 2017 Feb;147(2):269-284. doi: 10.1007/s00418-016-1513-9. Epub 2016 Nov 1. Histochem Cell Biol. 2017. PMID: 27803995 Review.
-
ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin.Mol Biol Cell. 1999 Aug;10(8):2573-82. doi: 10.1091/mbc.10.8.2573. Mol Biol Cell. 1999. PMID: 10436013 Free PMC article.
-
Minor folding defects trigger local modification of glycoproteins by the ER folding sensor GT.EMBO J. 2005 May 4;24(9):1730-8. doi: 10.1038/sj.emboj.7600645. Epub 2005 Apr 14. EMBO J. 2005. PMID: 15861139 Free PMC article.
-
Calnexin, More Than Just a Molecular Chaperone.Cells. 2023 Jan 24;12(3):403. doi: 10.3390/cells12030403. Cells. 2023. PMID: 36766745 Free PMC article. Review.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
