| | |  | | | | Record from Web of Science® | | | | | | |
| Glycosyltransferase activity of fringe modulates notch-delta interactions |
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| Author(s): Bruckner K, Perez L, Clausen H, Cohen S |
| Source: NATURE Volume: 406 Issue: 6794 Pages: 411-415 Published: JUL 27 2000 |
| Times Cited: 360 References: 30 |
| 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(1). Members of the fringe gene family have been implicated in limiting Notch activation during boundary formation(2-8), 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. |
| Document Type: Article |
| Language: English |
| Reprint Address: Cohen, S (reprint author), European Mol Biol Lab, Meyerhofstr 1, D-69117 Heidelberg, Germany |
Addresses:
1. European Mol Biol Lab, D-69117 Heidelberg, Germany
2. Univ Copenhagen, Sch Dent, DK-2200 Copenhagen N, Denmark |
| Publisher: MACMILLAN PUBLISHERS LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON N1 9XW, ENGLAND |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: 337WC |
| ISSN: 0028-0836 |
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