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Originally published In Press as doi:10.1074/jbc.M204445200 on May 29, 2002

J. Biol. Chem., Vol. 277, Issue 33, 29945-29952, August 16, 2002
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Notch Ligands Are Substrates for Protein O-Fucosyltransferase-1 and Fringe*

Vladislav M. PaninDagger §, Li Shao, Liang LeiDagger , Daniel J. Moloney||, Kenneth D. IrvineDagger , and Robert S. Haltiwanger**

From the Dagger  Howard Hughes Medical Institute, Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers, The State University, Piscataway, New Jersey 08854 and the  Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York, Stony Brook, New York 11794-5215

O-Fucose has been identified on epidermal growth factor-like (EGF) repeats of Notch, and elongation of O-fucose has been implicated in the modulation of Notch signaling by Fringe. O-Fucose modifications are also predicted to occur on Notch ligands based on the presence of the C2XXGG(S/T)C3 consensus site (where S/T is the modified amino acid) in a number of the EGF repeats of these proteins. Here we establish that both mammalian and Drosophila Notch ligands are modified with O-fucose glycans, demonstrating that the consensus site was useful for making predictions. The presence of O-fucose on Notch ligands raised the question of whether Fringe, an O-fucose specific beta 1,3-N-acetylglucosaminyltransferase, was capable of modifying O-fucose on the ligands. Indeed, O-fucose on mammalian Delta1 and Jagged1 can be elongated with Manic Fringe in vivo, and Drosophila Delta and Serrate are substrates for Drosophila Fringe in vitro. These results raise the interesting possibility that alteration of O-fucose glycans on Notch ligands could play a role in the mechanism of Fringe action on Notch signaling. As an initial step to begin addressing the role of the O-fucose glycans on Notch ligands in Notch signaling, a number of mutations in predicted O-fucose glycosylation sites on Drosophila Serrate have been generated. Interestingly, analysis of these mutants has revealed that O-fucose modifications occur on some EGF repeats not predicted by the C2XXGGS/TC3 consensus site. A revised, broad consensus site, C2X3-5S/TC3 (where X3-5 are any 3-5 amino acid residues), is proposed.

* This work was supported by National Institutes of Health Grants GM61126 (to R. S. H.) and GM54594 (to K. D. I.) and the Howard Hughes Medical Institute (to K. D. I.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: Dept. of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, TX 77843-2128.

|| Present address: Dept. of Cell Biology, Albert Einstein College of Medicine, 1300 Morris Park Ave., New York, NY 10461.

** To whom correspondence should be addressed. Tel: 631-632-7336; Fax: 631-632-8575; E-mail: Robert.Haltiwanger@SUNYSB.EDU.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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