ArticleScientific reports2017
Visualisation of a flexible modular structure of the ER folding-sensor enzyme UGGT.
Article in Scientific reports, 2017. 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, 47 citations in OpenAlex.
- N-glycan-dependent protein maturation and quality control in the ER.Nature reviews. Molecular cell biology · 2025Review
- The future of Asian biophysics built through Korea-Japan collaboration.Biophysics and physicobiology · 2025Article
- Insights into the interaction between UGGT, the gatekeeper of folding in the ER, and its partner, the selenoprotein SEP15.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Rescue of secretion of rare-disease-associated misfolded mutant glycoproteins in UGGT1 knock-out mammalian cells.Traffic (Copenhagen, Denmark) · 2024Article
- A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint.iScience · 2023Article
- Article
- Rescue of secretion of a rare-disease associated mis-folded mutant glycoprotein inbioRxiv : the preprint server for biology · 2023Article
- The introduction of an N-glycosylation site into prochymosin greatly enhances its production and secretion by Pichia pastoris.Microbial cell factories · 2022Article
- UDP-glucose, cereblon-dependent proinsulin degrader.Scientific reports · 2022Article
- JRAB/MICAL-L2 undergoes liquid-liquid phase separation to form tubular recycling endosomes.Communications biology · 2021Article
- Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase.Structure (London, England : 1993) · 2021Article
- The Role of Endoplasmic Reticulum Chaperones in Protein Folding and Quality Control.Progress in molecular and subcellular biology · 2021Article
- N-Glycosylation.Advances in experimental medicine and biology · 2021Article
- Article
- Calnexin cycle - structural features of the ER chaperone system.The FEBS journal · 2020Review
- Review
- UGGT1 retains proinsulin in the endoplasmic reticulum in an arginine dependent manner.Biochemical and biophysical research communications · 2020Article
- The Crucial Role of Demannosylating Asparagine-Linked Glycans in ERADicating Misfolded Glycoproteins in the Endoplasmic Reticulum.Frontiers in plant science · 2020Review
- Proper secretion of the serpin antithrombin relies strictly on thiol-dependent quality control.The Journal of biological chemistry · 2019Article
- Protein Quality Control in the Endoplasmic Reticulum.The protein journal · 2019Review
Corrections and comments
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Authors and funding
9 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the endoplasmic reticulum (ER), a protein quality control system facilitates the efficient folding of newly synthesised proteins. In this system, a series of N-linked glycan intermediates displayed on the protein surface serve as quality tags. The ER folding-sensor enzyme UDP-glucose:glycoprotein glucosyltransferase (UGGT) acts as a gatekeeper in the ER quality control system by specifically catalysing monoglucosylation onto incompletely folded glycoproteins, thereby enabling them to interact with lectin-chaperone complexes. Here we characterise the dynamic structure of this enzyme. Our crystallographic data demonstrate that the sensor region is composed of four thioredoxin-like domains followed by a β-rich domain, which are arranged into a C-shaped structure with a large central cavity, while the C-terminal catalytic domain undergoes a ligand-dependent conformational alteration. Furthermore, small-angle X-ray scattering, cryo-electron microscopy and high-speed atomic force microscopy have demonstrated that UGGT has a flexible modular structure in which the smaller catalytic domain is tethered to the larger folding-sensor region with variable spatial arrangements. These findings provide structural insights into the working mechanism whereby UGGT operates as a folding-sensor against a variety of glycoprotein substrates through its flexible modular structure possessing extended hydrophobic surfaces for the recognition of unfolded substrates.
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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.