ArticleThe Journal of biological chemistry2010
Two pathways for importing GDP-fucose into the endoplasmic reticulum lumen function redundantly in the O-fucosylation of Notch in Drosophila.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 52 citations in OpenAlex.
- Chemical Strategies to Custom-Modify α(1→3)-Fucosylated Glycan Motifs of the Human Glycocalyx.JACS Au · 2025Review
- The Memory Gene,Biomolecules · 2025Article
- Genetics of glycosylation in mammalian development and disease.Nature reviews. Genetics · 2024Review
- In vivo evidence for GDP-fucose transport in the absence of transporter SLC35C1 and putative transporter SLC35C2.The Journal of biological chemistry · 2023Article
- Fucose as a nutrient ligand for Dikarya and a building block of early diverging lineages.IMA fungus · 2023Article
- Delivery of Nucleotide Sugars to the Mammalian Golgi: A Very Well (un)Explained Story.International journal of molecular sciences · 2022Review
- POFUT1 acts as a tumor promoter in glioblastoma by enhancing the activation of Notch signaling.Journal of bioenergetics and biomembranes · 2021Article
- Therapeutic Monosaccharides: Looking Back, Moving Forward.Biochemistry · 2020Review
- Differential Labeling of Glycoproteins with Alkynyl Fucose Analogs.International journal of molecular sciences · 2020Article
- Down-regulation of SLC35C1 induces colon cancer through over-activating Wnt pathway.Journal of cellular and molecular medicine · 2020Article
- Article
- Nucleotide Sugar Transporter SLC35 Family Structure and Function.Computational and structural biotechnology journal · 2019Review
- Lysine at position 329 within a C-terminal dilysine motif is crucial for the ER localization of human SLC35B4.PloS one · 2018Article
- Biological functions of fucose in mammals.Glycobiology · 2017Review
- Dual Roles of O-Glucose Glycans Redundant with Monosaccharide O-Fucose on Notch in Notch Trafficking.The Journal of biological chemistry · 2016Article
- Phenotype-based clustering of glycosylation-related genes by RNAi-mediated gene silencing.Genes to cells : devoted to molecular & cellular mechanisms · 2015Article
- Dynamic regulation of innate immune responses in Drosophila by Senju-mediated glycosylation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Peters plus syndrome mutations disrupt a noncanonical ER quality-control mechanism.Current biology : CB · 2015Article
- Negative feedback regulation of Wnt signaling via N-linked fucosylation in zebrafish.Developmental biology · 2014Article
- In silico analysis of the fucosylation-associated genome of the human blood fluke Schistosoma mansoni: cloning and characterization of the enzymes involved in GDP-L-fucose synthesis and Golgi import.Parasites & vectors · 2013Article
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10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Notch is a transmembrane receptor that shares homology with proteins containing epidermal growth factor-like repeats and mediates the cell-cell interactions necessary for many cell fate decisions. In Drosophila, O-fucosyltransferase 1 catalyzes the O-fucosylation of these epidermal growth factor-like repeats. This O-fucose elongates, resulting in an O-linked tetrasaccharide that regulates the signaling activities of Notch. Fucosyltransferases utilize GDP-fucose, which is synthesized in the cytosol, but fucosylation occurs in the lumen of the endoplasmic reticulum (ER) and Golgi. Therefore, GDP-fucose uptake into the ER and Golgi is essential for fucosylation. However, although GDP-fucose biosynthesis is well understood, the mechanisms and intracellular routes of GDP-fucose transportation remain unclear. Our previous study on the Drosophila Golgi GDP-fucose transporter (Gfr), which specifically localizes to the Golgi, suggested that another GDP-fucose transporter(s) exists in Drosophila. Here, we identified Efr (ER GDP-fucose transporter), a GDP-fucose transporter that localizes specifically to the ER. Efr is a multifunctional nucleotide sugar transporter involved in the biosynthesis of heparan sulfate-glycosaminoglycan chains and the O-fucosylation of Notch. Comparison of the fucosylation defects in the N-glycans in Gfr and Efr mutants revealed that Gfr and Efr made distinct contributions to this modification; Gfr but not Efr was crucial for the fucosylation of N-glycans. We also found that Gfr and Efr function redundantly in the O-fucosylation of Notch, although they had different localizations and nucleotide sugar transportation specificities. These results indicate that two pathways for the nucleotide sugar supply, involving two nucleotide sugar transporters with distinct characteristics and distributions, contribute to the O-fucosylation of Notch.
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