ArticleThe Journal of biological chemistry2013
UDP-N-acetylglucosamine transporter (SLC35A3) regulates biosynthesis of highly branched N-glycans and keratan sulfate.
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 27 papers.
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27 citing papers in PubMed, 52 citations in OpenAlex.
- Noninferiority ofContrast media & molecular imaging · 2018Trial
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- Transcriptomic Adjustment to Decreasing Oxygen Reveals Novel Functional Strategies for Extreme Hypoxia Tolerance in the Copepod Tigriopus californicus.Genome biology and evolution · 2026Article
- Solute Carrier Family 35 A2 (SLC35A2) Promotes Tumor Progression through MYC-Mediated Pathways in Colorectal Cancer.International journal of medical sciences · 2025Article
- Protein Glycosylation Patterns Shaped By the IRE1-XBP1s Arm of the Unfolded Protein Response.Israel journal of chemistry · 2024Article
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- Delivery of Nucleotide Sugars to the Mammalian Golgi: A Very Well (un)Explained Story.International journal of molecular sciences · 2022Review
- Capture and metabolomic analysis of the human endometrial epithelial organoid secretome.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Integration of Sugar Metabolism and Proteoglycan Synthesis by UDP-glucose Dehydrogenase.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2021Review
- Chondrodysplasias With Multiple Dislocations Caused by Defects in Glycosaminoglycan Synthesis.Frontiers in genetics · 2021Review
- Biosynthesis of GlcNAc-richThe Journal of biological chemistry · 2020Article
- N-glycosylation of the human β1,4-galactosyltransferase 4 is crucial for its activity and Golgi localization.Glycoconjugate journal · 2020Article
- Therapeutic Monosaccharides: Looking Back, Moving Forward.Biochemistry · 2020Review
- Conserved Glu-47 and Lys-50 residues are critical for UDP-The Journal of biological chemistry · 2019Article
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- N-acetylglucosaminyltransferases and nucleotide sugar transporters form multi-enzyme-multi-transporter assemblies in golgi membranes in vivo.Cellular and molecular life sciences : CMLS · 2019Article
- SLC35A5 Protein-A Golgi Complex Member with Putative Nucleotide Sugar Transport Activity.International journal of molecular sciences · 2019Article
- XBP1s activation can globally remodel N-glycan structure distribution patterns.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Lysine at position 329 within a C-terminal dilysine motif is crucial for the ER localization of human SLC35B4.PloS one · 2018Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SLC35A3 is considered the main UDP-N-acetylglucosamine transporter (NGT) in mammals. Detailed analysis of NGT is restricted because mammalian mutant cells defective in this activity have not been isolated. Therefore, using the siRNA approach, we developed and characterized several NGT-deficient mammalian cell lines. CHO, CHO-Lec8, and HeLa cells deficient in NGT activity displayed a decrease in the amount of highly branched tri- and tetraantennary N-glycans, whereas monoantennary and diantennary ones remained unchanged or even were accumulated. Silencing the expression of NGT in Madin-Darby canine kidney II cells resulted in a dramatic decrease in the keratan sulfate content, whereas no changes in biosynthesis of heparan sulfate were observed. We also demonstrated for the first time close proximity between NGT and mannosyl (α-1,6-)-glycoprotein β-1,6-N-acetylglucosaminyltransferase (Mgat5) in the Golgi membrane. We conclude that NGT may be important for the biosynthesis of highly branched, multiantennary complex N-glycans and keratan sulfate. We hypothesize that NGT may specifically supply β-1,3-N-acetylglucosaminyl-transferase 7 (β3GnT7), Mgat5, and possibly mannosyl (α-1,3-)-glycoprotein β-1,4-N-acetylglucosaminyltransferase (Mgat4) with UDP-GlcNAc.
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