Fringe is a glycosyltransferase that modifies Notch

Daniel J. Moloney, Vladislav M. Panin, Stuart H. Johnston, Jihua Chen, Li Shao, Richa Wilson, Yang Wang, Pamela Stanley (), Kenneth D. Irvine (), Robert S. Haltiwanger () and Thomas F. Vogt ()
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Daniel J. Moloney: Institute for Cell and Developmental Biology
Vladislav M. Panin: Rutgers, The State University
Stuart H. Johnston: Princeton
Jihua Chen: Albert Einstein College of Medicine
Li Shao: Institute for Cell and Developmental Biology
Richa Wilson: Rutgers, The State University
Yang Wang: Genentech, Inc.
Pamela Stanley: Albert Einstein College of Medicine
Kenneth D. Irvine: Rutgers, The State University
Robert S. Haltiwanger: Institute for Cell and Developmental Biology
Thomas F. Vogt: Princeton

Nature, 2000, vol. 406, issue 6794, 369-375

Abstract: Abstract Notch receptors function in highly conserved intercellular signalling pathways that direct cell-fate decisions, proliferation and apoptosis in metazoans. Fringe proteins can positively and negatively modulate the ability of Notch ligands to activate the Notch receptor. Here we establish the biochemical mechanism of Fringe action. Drosophila and mammalian Fringe proteins possess a fucose-specific β1,3 N-acetylglucosaminyltransferase activity that initiates elongation of O-linked fucose residues attached to epidermal growth factor-like sequence repeats of Notch. We obtained biological evidence that Fringe-dependent elongation of O-linked fucose on Notch modulates Notch signalling by using co-culture assays in mammalian cells and by expression of an enzymatically inactive Fringe mutant in Drosophila . The post-translational modification of Notch by Fringe represents a striking example of modulation of a signalling event by differential receptor glycosylation and identifies a mechanism that is likely to be relevant to other signalling pathways.

Date: 2000
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DOI: 10.1038/35019000

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