Glycosyltransferase activity of Fringe modulates Notch-Delta interactions - PubMed (original) (raw)
. 2000 Jul 27;406(6794):411-5.
doi: 10.1038/35019075.
Affiliations
- PMID: 10935637
- DOI: 10.1038/35019075
Glycosyltransferase activity of Fringe modulates Notch-Delta interactions
K Brückner et al. Nature. 2000.
Erratum in
- Nature 2000 Oct 5;407(6804):654
Abstract
Ligands that are capable of activating Notch family receptors are broadly expressed in animal development, but their activity is tightly regulated to allow formation of tissue boundaries. Members of the fringe gene family have been implicated in limiting Notch activation during boundary formation, but the mechanism of Fringe function has not been determined. Here we present evidence that Fringe acts in the Golgi as a glycosyltransferase enzyme that modifies the epidermal growth factor (EGF) modules of Notch and alters the ability of Notch to bind its ligand Delta. Fringe catalyses the addition of N-acetylglucosamine to fucose, which is consistent with a role in the elongation of O-linked fucose O-glycosylation that is associated with EGF repeats. We suggest that cell-type-specific modification of glycosylation may provide a general mechanism to regulate ligand-receptor interactions in vivo.
Comment in
- Fringe benefits to carbohydrates.
Fortini ME. Fortini ME. Nature. 2000 Jul 27;406(6794):357-8. doi: 10.1038/35019233. Nature. 2000. PMID: 10935619 No abstract available.
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