ArticlePloS one2014
O-fucosylation of the notch ligand mDLL1 by POFUT1 is dispensable for ligand function.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 37 citations in OpenAlex.
- Structure, function, and implications of fucosyltransferases in health and disease.Nature communications · 2025Review
- POFUT1 as a cancer biomarker: insights into its oncogenic mechanisms and clinical relevance.Journal of molecular medicine (Berlin, Germany) · 2025Review
- ProteinMolecules (Basel, Switzerland) · 2025Review
- Lfng and Dll3 cooperate to modulate protein interactions in cis and coordinate oscillatory Notch pathway activation in the segmentation clock.Developmental biology · 2022Article
- Research progress on O-GlcNAcylation in the occurrence, development, and treatment of colorectal cancer.World journal of gastrointestinal surgery · 2021Review
- Current Views on the Roles ofBiomolecules · 2021Review
- Multifaceted regulation of Notch signaling by glycosylation.Glycobiology · 2021Review
- Article
- Decoding the PTM-switchboard of Notch.Biochimica et biophysica acta. Molecular cell research · 2019Review
- Multiple roles for O-glycans in Notch signalling.FEBS letters · 2018Review
- Article
- Congenital diseases caused by defectiveNagoya journal of medical science · 2018Review
- Inhibition of Delta-induced Notch signaling using fucose analogs.Nature chemical biology · 2018Article
- The Function of Fucosylation in Progression of Lung Cancer.Frontiers in oncology · 2018Review
- Notch Ligand Binding Assay Using Flow Cytometry.Bio-protocol · 2017Article
- Predicting the Retention Behavior of SpecificJournal of biomolecular techniques : JBT · 2017Article
- Biological functions of fucose in mammals.Glycobiology · 2017Review
- Deletion ofMolecular and cellular biology · 2017Article
- Article
- Reduced Notch signalling leads to postnatal skeletal muscle hypertrophy in Pofut1cax/cax mice.Open biology · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Fucosylation of Epidermal Growth Factor-like (EGF) repeats by protein O-fucosyltransferase 1 (POFUT1 in vertebrates, OFUT1 in Drosophila) is pivotal for NOTCH function. In Drosophila OFUT1 also acts as chaperone for Notch independent from its enzymatic activity. NOTCH ligands are also substrates for POFUT1, but in Drosophila OFUT1 is not essential for ligand function. In vertebrates the significance of POFUT1 for ligand function and subcellular localization is unclear. Here, we analyze the importance of O-fucosylation and POFUT1 for the mouse NOTCH ligand Delta-like 1 (DLL1). We show by mass spectral glycoproteomic analyses that DLL1 is O-fucosylated at the consensus motif C²XXXX(S/T)C³ (where C² and C³ are the second and third conserved cysteines within the EGF repeats) found in EGF repeats 3, 4, 7 and 8. A putative site with only three amino acids between the second cysteine and the hydroxy amino acid within EGF repeat 2 is not modified. DLL1 proteins with mutated O-fucosylation sites reach the cell surface and accumulate intracellularly. Likewise, in presomitic mesoderm cells of POFUT1 deficient embryos DLL1 is present on the cell surface, and in mouse embryonic fibroblasts lacking POFUT1 the same relative amount of overexpressed wild type DLL1 reaches the cell surface as in wild type embryonic fibroblasts. DLL1 expressed in POFUT1 mutant cells can activate NOTCH, indicating that POFUT1 is not required for DLL1 function as a Notch ligand.
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Registered trials
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.