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A more recent version of this article appeared on August 26, 2005
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Papers In Press, published online ahead of print June 30, 2005
J. Biol. Chem, 10.1074/jbc.M505569200
Submitted on May 20, 2005
Accepted on June 30, 2005

Regions of Drosophila notch that contribute to ligand binding and the modulatory influence of fringe

Aiguo Xu, Liang Lei, and Kenneth D. Irvine

HHMI, Waksman Institute, Rutgers University, Piscataway, NJ 08854

Corresponding Author: irvine{at}waksman.rutgers.edu

Two glycosyltransferases that transfer sugars to EGF domains, OFUT1 and Fringe, regulate Notch signaling. To characterize the impact of glycosylation at the 23 consensus O-fucose sites in Drosophila Notch, we conducted deletion mapping and site-specific mutagenesis, and then assayed the binding of soluble forms of Notch to cell-surface ligands. Our results support the conclusion that EGF domains 11 and 12 are essential for ligand binding, but indicate that other EGF domains also make substantial contributions to ligand binding. Characterization of Notch deletion constructs and O-fucose site mutants further reveals that no single site or region can account for the influence of Fringe on Notch-ligand binding. Additionally, an influence of Fringe can be observed on a Notch fragment that includes only four of its thirty-six EGF domains (EGF10-13). Together, our observations imply that glycosylation influences Notch-ligand interactions through a distributive mechanism that involves local interactions with multiple EGF domains, and lead us to suggest a structural model for how Notch interacts with its ligands.


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