ArticleMolecular biology of the cell2003
Association of the Golgi UDP-galactose transporter with UDP-galactose:ceramide galactosyltransferase allows UDP-galactose import in the endoplasmic reticulum.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 105 citations in OpenAlex.
- Neuromuscular Defects in aBiomolecules · 2025Article
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- Loss of Slc35a2 alters development of the mouse cerebral cortex.Neuroscience letters · 2024Article
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- A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint.iScience · 2023Article
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- 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
- Nucleotide sugar transporter SLC35A2 is involved in promoting hepatocellular carcinoma metastasis by regulating cellular glycosylation.Cellular oncology (Dordrecht, Netherlands) · 2023Article
- Delivery of Nucleotide Sugars to the Mammalian Golgi: A Very Well (un)Explained Story.International journal of molecular sciences · 2022Review
- Article
- Glucosylceramide and galactosylceramide, small glycosphingolipids with significant impact on health and disease.Glycobiology · 2021Review
- Functional analyses of the UDP-galactose transporter SLC35A2 using the binding of bacterial Shiga toxins as a novel activity assay.Glycobiology · 2019Article
- Developmental Comparison of Ceramide in Wild-Type andFrontiers in neurology · 2019Article
- Lysine at position 329 within a C-terminal dilysine motif is crucial for the ER localization of human SLC35B4.PloS one · 2018Article
- Galactose Supplementation in Patients With TMEM165-CDG Rescues the Glycosylation Defects.The Journal of clinical endocrinology and metabolism · 2017Article
- Glycosphingolipid-Protein Interaction in Signal Transduction.International journal of molecular sciences · 2016Review
- UDP-galactose and acetyl-CoA transporters as Plasmodium multidrug resistance genes.Nature microbiology · 2016Article
- A new case of UDP-galactose transporter deficiency (SLC35A2-CDG): molecular basis, clinical phenotype, and therapeutic approach.Journal of inherited metabolic disease · 2015Article
- Determinants of Glycosaminoglycan (GAG) Structure.Biomolecules · 2015Review
- UDP-galactose (SLC35A2) and UDP-N-acetylglucosamine (SLC35A3) Transporters Form Glycosylation-related Complexes with Mannoside Acetylglucosaminyltransferases (Mgats).The Journal of biological chemistry · 2015Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
UDP-galactose reaches the Golgi lumen through the UDP-galactose transporter (UGT) and is used for the galactosylation of proteins and lipids. Ceramides and diglycerides are galactosylated within the endoplasmic reticulum by the UDP-galactose:ceramide galactosyltransferase. It is not known how UDP-galactose is transported from the cytosol into the endoplasmic reticulum. We transfected ceramide galactosyltransferase cDNA into CHOlec8 cells, which have a defective UGT and no endogenous ceramide galactosyltransferase. Cotransfection with the human UGT1 greatly stimulated synthesis of lactosylceramide in the Golgi and of galactosylceramide in the endoplasmic reticulum. UDP-galactose was directly imported into the endoplasmic reticulum because transfection with UGT significantly enhanced synthesis of galactosylceramide in endoplasmic reticulum membranes. Subcellular fractionation and double label immunofluorescence microscopy showed that a sizeable fraction of ectopically expressed UGT and ceramide galactosyltransferase resided in the endoplasmic reticulum of CHOlec8 cells. The same was observed when UGT was expressed in human intestinal cells that have an endogenous ceramide galactosyltransferase. In contrast, in CHOlec8 singly transfected with UGT 1, the transporter localized exclusively to the Golgi complex. UGT and ceramide galactosyltransferase were entirely detergent soluble and form a complex because they could be coimmunoprecipitated. We conclude that the ceramide galactosyltransferase ensures a supply of UDP-galactose in the endoplasmic reticulum lumen by retaining UGT in a molecular complex.
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