ArticleThe Journal of biological chemistry2015
UDP-galactose (SLC35A2) and UDP-N-acetylglucosamine (SLC35A3) Transporters Form Glycosylation-related Complexes with Mannoside Acetylglucosaminyltransferases (Mgats).
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.
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Who cites it
28 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.
- Association of UGT1A1*6 polymorphism with irinotecan-based chemotherapy reaction in colorectal cancer patients: a systematic review and a meta-analysis.Bioscience reports · 2020Pooled it
- Structural Characterization of Glycoprotein Glycans and Glycosaminoglycans of Brain Tissues inInternational journal of molecular sciences · 2026Article
- Evolutionary analyses of the animal glycosyltransferase family 54 reveals two β1,4-N-acetylglucosaminyltransferase families.iScience · 2025Article
- Neuromuscular Defects in aBiomolecules · 2025Article
- Structure of the Secretory Compartments in Goblet Cells in the Colon and Small Intestine.Cells · 2025Article
- Human brain tissue with MOGHE carrying somatic SLC35A2 variants reveal aberrant protein expression and protein loss in the white matter.Acta neuropathologica · 2025Article
- The role of UGT1A1 polymorphism in the management of colorectal cancer.Oncology reviews · 2025Review
- Cytosolic UDP-Gal biosynthetic machinery is required for dimerization of SLC35A2 in the Golgi membrane and its interaction with B4GalT1.Frontiers in molecular biosciences · 2025Article
- Golgi-IP, a tool for multimodal analysis of Golgi molecular content.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Screening of Membrane Protein Production by Comparison of Transient Expression in Insect and Mammalian Cells.Biomolecules · 2023Article
- Article
- Comprehensive Analysis Identified Glycosyltransferase Signature to Predict Glioma Prognosis and TAM Phenotype.BioMed research international · 2023Article
- Delivery of Nucleotide Sugars to the Mammalian Golgi: A Very Well (un)Explained Story.International journal of molecular sciences · 2022Review
- Article
- Strategies for Successful Over-Expression of Human Membrane Transport Systems Using Bacterial Hosts: Future Perspectives.International journal of molecular sciences · 2022Review
- Novel Insights into Selected Disease-Causing Mutations within theInternational journal of molecular sciences · 2020Article
- Biosynthesis of GlcNAc-richThe Journal of biological chemistry · 2020Article
- Detection of rs665862918 (15-bp Indel) of theAnimals : an open access journal from MDPI · 2020Article
- Conserved Glu-47 and Lys-50 residues are critical for UDP-The Journal of biological chemistry · 2019Article
- N-acetylglucosaminyltransferases and nucleotide sugar transporters form multi-enzyme-multi-transporter assemblies in golgi membranes in vivo.Cellular and molecular life sciences : CMLS · 2019Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
UDP-galactose transporter (UGT; SLC35A2) and UDP-N-acetylglucosamine transporter (NGT; SLC35A3) form heterologous complexes in the Golgi membrane. NGT occurs in close proximity to mannosyl (α-1,6-)-glycoprotein β-1,6-N-acetylglucosaminyltransferase (Mgat5). In this study we analyzed whether NGT and both splice variants of UGT (UGT1 and UGT2) are able to interact with four different mannoside acetylglucosaminyltransferases (Mgat1, Mgat2, Mgat4B, and Mgat5). Using an in situ proximity ligation assay, we found that all examined glycosyltransferases are in the vicinity of these UDP-sugar transporters both at the endogenous level and upon overexpression. This observation was confirmed via the FLIM-FRET approach for both NGT and UGT1 complexes with Mgats. This study reports for the first time close proximity between endogenous nucleotide sugar transporters and glycosyltransferases. We also observed that among all analyzed Mgats, only Mgat4B occurs in close proximity to UGT2, whereas the other three Mgats are more distant from UGT2, and it was only possible to visualize their vicinity using proximity ligation assay. This strongly suggests that the distance between these protein pairs is longer than 10 nm but at the same time shorter than 40 nm. This study adds to the understanding of glycosylation, one of the most important post-translational modifications, which affects the majority of macromolecules. Our research shows that complex formation between nucleotide sugar transporters and glycosyltransferases might be a more common phenomenon than previously thought.
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