Glycosylation of Pre-Notch by Fringe

Stable Identifier
R-MMU-2023158
Type
Reaction [transition]
Species
Mus musculus
Compartment
General
SVG |   | PPTX  | SBGN
Glycosylation of Pre-Notch by Fringe

Mouse Notch1 fragment containing EGF repeats 19-23, with a conserved O-fucosylation site in EGF repeat 20, was shown to be a direct target of manic fringe (Mfng) when both mouse Notch1 fragment and Mfng were exogenously expressed in a Chinese hamster ovary cell line (Moloney et al. 2000). Lunatic fringe was shown to directly act on Notch1 to modulate its signaling (Hicks et al. 2000). Fringe enzymes include lunatic fringe (Lfng), manic fringe (Mfng) and radical fringe (Rfng) in mammals. Fringe enzymes localize to Golgi membrane and function by extending O-fucosyl residues on fucosylated peptides, including Notch, by transferring a beta 1,3-linked N-acetyl glucosaminyl group. Since the exact preference, if any, of fringe enzymes for Notch O-fucose sites is not known, the extension of an O-fucosyl residue at unknown position is shown.

Literature References
PubMed ID Title Journal Year
9207795 Fringe boundaries coincide with Notch-dependent patterning centres in mammals and alter Notch-dependent development in Drosophila

Cohen, B, Bashirullah, A, Dagnino, L, Campbell, C, Fisher, WW, Leow, CC, Whiting, E, Ryan, D, Zinyk, D, Boulianne, G, Hui, CC, Gallie, B, Phillips, RA, Lipshitz, HD, Egan, SE

Nat Genet 1997
10935626 Fringe is a glycosyltransferase that modifies Notch

Moloney, DJ, Panin, VM, Johnston, SH, Chen, J, Shao, L, Wilson, R, Wang, Y, Stanley, P, Irvine, KD, Haltiwanger, RS, Vogt, TF

Nature 2000
9187150 A family of mammalian Fringe genes implicated in boundary determination and the Notch pathway

Johnston, SH, Rauskolb, C, Wilson, R, Prabhakaran, B, Irvine, KD, Vogt, TF

Development 1997
Participants
Catalyst Activity
Catalyst Activity
Title
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity of Fringe [Golgi membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created