Glycosyltransferase activity of Fringe modulates Notch–Delta interactions

Katja Brückner, Lidia Perez, Henrik Clausen and Stephen Cohen ()
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Katja Brückner: European Molecular Biology Laboratory
Lidia Perez: European Molecular Biology Laboratory
Henrik Clausen: School of Dentistry, University of Copenhagen
Stephen Cohen: European Molecular Biology Laboratory

Nature, 2000, vol. 406, issue 6794, 411-415

Abstract: 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 boundaries1. Members of the fringe gene family have been implicated in limiting Notch activation during boundary formation2,3,4,5,6,7,8, 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.

Date: 2000
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DOI: 10.1038/35019075

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