ArticleThe Journal of biological chemistry2013
Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- Structures of the mannose-6-phosphate pathway enzyme, GlcNAc-1-phosphotransferase.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- GANAB andInternational journal of molecular sciences · 2022Review
- PRKCSH contributes to tumorigenesis by selective boosting of IRE1 signaling pathway.Nature communications · 2019Article
- Characterizing the selectivity of ER α-glucosidase inhibitors.Glycobiology · 2019Article
- 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
- Processing of the Terminal Alpha-1,2-Linked Mannose Residues From OligomannosidicFrontiers in plant science · 2018Article
- 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
- Enzyme-specific differences in mannose phosphorylation between GlcNAc-1-phosphotransferase αβ and γ subunit deficient zebrafish support cathepsin proteases as early mediators of mucolipidosis pathology.Biochimica et biophysica acta · 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
- Iminosugars Inhibit Dengue Virus Production via Inhibition of ER Alpha-Glucosidases--Not Glycolipid Processing Enzymes.PLoS neglected tropical diseases · 2016Article
- Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control.Scientific reports · 2016Article
- 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
- Identification of a fourth mannose 6-phosphate binding site in the cation-independent mannose 6-phosphate receptor.Glycobiology · 2015Article
- Emerging structural insights into glycoprotein quality control coupled with N-glycan processing in the endoplasmic reticulum.Molecules (Basel, Switzerland) · 2015Review
- Glucosidase II and MRH-domain containing proteins in the secretory pathway.Current protein & peptide science · 2015Review
- Convergent and divergent mechanisms of sugar recognition across kingdoms.Current opinion in structural biology · 2014Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Here we report for the first time the three-dimensional structure of a mannose 6-phosphate receptor homology (MRH) domain present in a protein with enzymatic activity, glucosidase II (GII). GII is involved in glycoprotein folding in the endoplasmic reticulum. GII removes the two innermost glucose residues from the Glc3Man9GlcNAc2 transferred to nascent proteins and the glucose added by UDP-Glc:glycoprotein glucosyltransferase. GII is composed of a catalytic GIIα subunit and a regulatory GIIβ subunit. GIIβ participates in the endoplasmic reticulum localization of GIIα and mediates in vivo enhancement of N-glycan trimming by GII through its C-terminal MRH domain. We determined the structure of a functional GIIβ MRH domain by NMR spectroscopy. It adopts a β-barrel fold similar to that of other MRH domains, but its binding pocket is the most shallow known to date as it accommodates a single mannose residue. In addition, we identified a conserved residue outside the binding pocket (Trp-409) present in GIIβ but not in other MRHs that influences GII glucose trimming activity.
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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.