ArticleProceedings of the National Academy of Sciences of the United States of America2001
Physical and functional association of glycolipid N-acetyl-galactosaminyl and galactosyl transferases in the Golgi apparatus.
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 47 papers.
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47 citing papers in PubMed, 132 citations in OpenAlex.
- Vesicular trafficking and cell-cell communication in neurodevelopment and neurodegeneration.Frontiers in cell and developmental biology · 2025Review
- Deciphering mouse brain spatial diversity via glyco-lipidomic mapping.Nature communications · 2024Article
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- Ganglioside GM1 and the Central Nervous System.International journal of molecular sciences · 2023Review
- Synthesis, Processing, and Function of N-Glycans in N-Glycoproteins.Advances in neurobiology · 2023Review
- Golgi Phosphoprotein 3 Regulates the Physical Association of Glycolipid Glycosyltransferases.International journal of molecular sciences · 2022Article
- Cancer-Associated Glycosphingolipids as Tumor Markers and Targets for Cancer Immunotherapy.International journal of molecular sciences · 2021Review
- ATP-binding cassette transporters mediate differential biosynthesis of glycosphingolipid species.Journal of lipid research · 2021Article
- Gangliosides and Neuroblastomas.International journal of molecular sciences · 2020Review
- Cross-talks of glycosylphosphatidylinositol biosynthesis with glycosphingolipid biosynthesis and ER-associated degradation.Nature communications · 2020Article
- Ganglioside Synthesis by Plasma Membrane-Associated Sialyltransferase in Macrophages.International journal of molecular sciences · 2020Article
- Article
- Composition, Assembly, and Trafficking of a Wheat Xylan Synthase Complex.Plant physiology · 2016Article
- Glycosyltransferase complexes in eukaryotes: long-known, prevalent but still unrecognized.Cellular and molecular life sciences : CMLS · 2016Review
- Time-resolved fluorescence imaging reveals differential interactions of N-glycan processing enzymes across the Golgi stack in planta.Plant physiology · 2013Article
- 2-Bromopalmitate reduces protein deacylation by inhibition of acyl-protein thioesterase enzymatic activities.PloS one · 2013Article
- Spatial organization and stoichiometry of N-terminal domain-mediated glycosyltransferase complexes in Golgi membranes determined by fret microscopy.Neurochemical research · 2012Article
- Ganglioside biochemistry.ISRN biochemistry · 2012Review
- Quantitative transcriptomic profiling of branching in a glycosphingolipid biosynthetic pathway.The Journal of biological chemistry · 2011Article
- Mechanisms of protein retention in the Golgi.Cold Spring Harbor perspectives in biology · 2011Review
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3 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Glycolipid glycosyltransferases catalyze the stepwise transfer of monosaccharides from sugar nucleotides to proper glycolipid acceptors. They are Golgi resident proteins that colocalize functionally in the organelle, but their intimate relationships are not known. Here, we show that the sequentially acting UDP-GalNAc:lactosylceramide/GM3/GD3 beta-1,4-N-acetyl-galactosaminyltransferase and the UDP-Gal:GA2/GM2/GD2 beta-1,3-galactosyltransferase associate physically in the distal Golgi. Immunoprecipitation of the respective epitope-tagged versions expressed in transfected CHO-K1 cells resulted in their mutual coimmunoprecipitation. The immunocomplexes efficiently catalyze the two transfer steps leading to the synthesis of GM1 from exogenous GM3 in the presence of UDP-GalNAc and UDP-Gal. The N-terminal domains (cytosolic tail, transmembrane domain, and few amino acids of the stem region) of both enzymes are involved in the interaction because (i) they reproduce the coimmunoprecipitation behavior of the full-length enzymes, (ii) they compete with the full-length counterpart in both coimmunoprecipitation and GM1 synthesis experiments, and (iii) fused to the cyan and yellow fluorescent proteins, they localize these proteins to the Golgi membranes in an association close enough as to allow fluorescence resonance energy transfer between them. We suggest that these associations may improve the efficiency of glycolipid synthesis by channeling the intermediates from the position of product to the position of acceptor along the transfer steps.
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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.