ArticleThe Journal of cell biology2010
The role of UDP-Glc:glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin.
Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed, 44 citations in OpenAlex.
- UGGT1-mediated reglucosylation ofeLife · 2024Article
- Rescue of secretion of rare-disease-associated misfolded mutant glycoproteins in UGGT1 knock-out mammalian cells.Traffic (Copenhagen, Denmark) · 2024Article
- ER chaperones use a protein folding and quality control glyco-code.Molecular cell · 2023Article
- Rescue of secretion of a rare-disease associated mis-folded mutant glycoprotein inbioRxiv : the preprint server for biology · 2023Article
- Article
- 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
- Modulation of ERQC and ERAD: A Broad-Spectrum Spanner in the Works of Cancer Cells?Journal of oncology · 2019Review
- Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- 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
- Reduced expression of the oligosaccharyltransferase exacerbates protein hypoglycosylation in cells lacking the fully assembled oligosaccharide donor.Glycobiology · 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
- The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis.Nature chemical biology · 2014Review
- Endoplasmic reticulum glycoprotein quality control regulates CD1d assembly and CD1d-mediated antigen presentation.The Journal of biological chemistry · 2013Article
- Protein folding in the endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013Review
- Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis.Trends in biochemical sciences · 2012Article
- Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems.Current opinion in cell biology · 2011Review
- ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER.Current opinion in cell biology · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
An endoplasmic reticulum (ER) quality control system assists in efficient folding and disposal of misfolded proteins. N-linked glycans are critical in these events because their composition dictates interactions with molecular chaperones. UDP-glucose:glycoprotein glucosyltransferase 1 (UGT1) is a key quality control factor of the ER. It adds glucoses to N-linked glycans of nonglucosylated substrates that fail a quality control test, supporting additional rounds of chaperone binding and ER retention. How UGT1 functions in its native environment is poorly understood. The role of UGT1 in the maturation of glycoproteins at basal expression levels was analyzed. Prosaposin was identified as a prominent endogenous UGT1 substrate. A dramatic decrease in the secretion of prosaposin was observed in ugt1(-/-) cells with prosaposin localized to large juxtanuclear aggresome-like inclusions, which is indicative of its misfolding and the essential role that UGT1 plays in its proper maturation. A model is proposed that explains how UGT1 may aid in the folding of sequential domain-containing proteins such as prosaposin.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.