ArticleProceedings of the National Academy of Sciences of the United States of America2001
Immunolocalization of UDP-glucose:glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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.
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Who cites it
38 citing papers in PubMed, 86 citations in OpenAlex.
- The ER-Golgi intermediate compartment: a central hub integrating membrane trafficking and stress responses.EMBO reports · 2026Review
- N-glycan-dependent protein maturation and quality control in the ER.Nature reviews. Molecular cell biology · 2025Review
- TTC17 is an endoplasmic reticulum resident TPR-containing adaptor protein.The Journal of biological chemistry · 2023Article
- In vivo characterization of Drosophila golgins reveals redundancy and plasticity of vesicle capture at the Golgi apparatus.Current biology : CB · 2022Article
- The IRE1α pathway in glomerular diseases: The unfolded protein response and beyond.Frontiers in molecular medicine · 2022Review
- Visualization of Procollagen IV Reveals ER-to-Golgi Transport by ERGIC-independent Carriers.Cell structure and function · 2020Article
- Intermediate compartment (IC): from pre-Golgi vacuoles to a semi-autonomous membrane system.Histochemistry and cell biology · 2018Review
- Role of Selenof as a Gatekeeper of Secreted Disulfide-Rich Glycoproteins.Cell reports · 2018Article
- 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
- Article
- Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9.Histochemistry and cell biology · 2017Review
- N-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding Cycle.Traffic (Copenhagen, Denmark) · 2016Review
- A novel UGGT1 and p97-dependent checkpoint for native ectodomains with ionizable intramembrane residue.Molecular biology of the cell · 2015Article
- Reglucosylation by UDP-glucose:glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation.Molecular biology of the cell · 2015Article
- Glucosidase II and MRH-domain containing proteins in the secretory pathway.Current protein & peptide science · 2015Review
- Rab2A is a pivotal switch protein that promotes either secretion or ER-associated degradation of (pro)insulin in insulin-secreting cells.Scientific reports · 2014Article
- The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis.Nature chemical biology · 2014Review
- ERADication of EDEM1 occurs by selective autophagy and requires deglycosylation by cytoplasmic peptide N-glycanase.Histochemistry and cell biology · 2014Article
- Ca2+-activated nucleotidase 1, a novel target gene for the transcriptional repressor DREAM (downstream regulatory element antagonist modulator), is involved in protein folding and degradation.The Journal of biological chemistry · 2012Article
- Sorting things out through endoplasmic reticulum quality control.Molecular membrane biology · 2010Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
The UDP-glucose:glycoprotein glucosyltransferase (GT) is a protein folding sensor and glycosyltransferase that constitutes an important component of the protein quality control machinery. With the use of quantitative immunogold electron microscopy, we established the subcellular distribution of GT in rat liver and pancreas and Drosophila melanogaster salivary gland as well as cell lines and correlated it with that of glucosidase II, calreticulin, and pre-Golgi intermediate markers. Labeling for GT, as well as for glucosidase II and calreticulin, was found in the endoplasmic reticulum (ER), including nuclear envelope and pre-Golgi intermediates located between ER and Golgi apparatus, and in the cell periphery. In the rough ER, labeling for GT was inhomogeneous, with variously sized labeled and unlabeled cisternal regions alternating, indicative of a meshwork of quality control checkpoints. Notably, labeling intensity for GT was highest in pre-Golgi intermediates, corresponding to twice that of rough ER, whereas the Golgi apparatus exhibited no specific labeling. These results suggest that protein quality control is not restricted to the ER and that the pre-Golgi intermediates, by virtue of the presence of GT, glucosidase II, and calreticulin, are involved in this fundamental cellular process.
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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.