ArticleMolecular biology of the cell2011
Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 45 citations in OpenAlex.
- Combinatory glycoengineering of monoclonal antibodies and its application in cancer therapy: a narrative review.Translational cancer research · 2024Review
- Analysis of Lipid-linked Oligosaccharides SynthesizedBio-protocol · 2022Article
- A Non-redundant Function of MNS5: A Class I α-1, 2 Mannosidase, in the Regulation of Endoplasmic Reticulum-Associated Degradation of Misfolded Glycoproteins.Frontiers in plant science · 2022Article
- Abrogation of glucosidase I-mediated glycoprotein deglucosylation results in a sick phenotype in fission yeasts: Model for the human MOGS-CDG disorder.The Journal of biological chemistry · 2018Article
- Structural investigation of glycan recognition by the ERAD quality control lectin Yos9.Journal of biomolecular NMR · 2018Article
- Protein Quality Control in the Endoplasmic Reticulum of Plants.Annual review of plant biology · 2018Review
- Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control.Protein science : a publication of the Protein Society · 2016Article
- Structures of mammalian ER α-glucosidase II capture the binding modes of broad-spectrum iminosugar antivirals.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- N-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding Cycle.Traffic (Copenhagen, Denmark) · 2016Review
- Thyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology.Endocrine reviews · 2016Review
- Article
- Glycoprotein Quality Control and Endoplasmic Reticulum Stress.Molecules (Basel, Switzerland) · 2015Review
- Crystal Structure and Functional Analyses of the Lectin Domain of Glucosidase II: Insights into Oligomannose Recognition.Biochemistry · 2015Article
- The UDP-glucose: glycoprotein glucosyltransferase (UGGT), a key enzyme in ER quality control, plays a significant role in plant growth as well as biotic and abiotic stress in Arabidopsis thaliana.BMC plant biology · 2015Article
- N-linked sugar-regulated protein folding and quality control in the ER.Seminars in cell & developmental biology · 2015Review
- Reglucosylation by UDP-glucose:glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation.Molecular biology of the cell · 2015Article
- Mammalian ER mannosidase I resides in quality control vesicles, where it encounters its glycoprotein substrates.Molecular biology of the cell · 2015Article
- Expression of α-subunit of α-glucosidase II in adult mouse brain regions and selected organs.Journal of neuroscience research · 2015Article
- Glucosidase II and MRH-domain containing proteins in the secretory pathway.Current protein & peptide science · 2015Review
- A context-independent N-glycan signal targets the misfolded extracellular domain of Arabidopsis STRUBBELIG to endoplasmic-reticulum-associated degradation.The Biochemical journal · 2014Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Glucosidase II (GII) sequentially removes the two innermost glucose residues from the glycan (Glc(3)Man(9)GlcNAc(2)) transferred to proteins. GII also participates in cycles involving the lectin/chaperones calnexin (CNX) and calreticulin (CRT) as it removes the single glucose unit added to folding intermediates and misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase (UGGT). GII is a heterodimer in which the α subunit (GIIα) bears the active site, and the β subunit (GIIβ) modulates GIIα activity through its C-terminal mannose 6-phosphate receptor homologous (MRH) domain. Here we report that, as already described in cell-free assays, in live Schizosaccharomyces pombe cells a decrease in the number of mannoses in the glycan results in decreased GII activity. Contrary to previously reported cell-free experiments, however, no such effect was observed in vivo for UGGT. We propose that endoplasmic reticulum α-mannosidase-mediated N-glycan demannosylation of misfolded/slow-folding glycoproteins may favor their interaction with the lectin/chaperone CNX present in S. pombe by prolonging the half-lives of the monoglucosylated glycans (S. pombe lacks CRT). Moreover, we show that even N-glycans bearing five mannoses may interact in vivo with the GIIβ MRH domain and that the N-terminal GIIβ G2B domain is involved in the GIIα-GIIβ interaction. Finally, we report that protists that transfer glycans with low mannose content to proteins have nevertheless conserved the possibility of displaying relatively long-lived monoglucosylated glycans by expressing GIIβ MRH domains with a higher specificity for glycans with high mannose content.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.