title: Fringe boundaries coincide with Notch-dependent patterning centres in mammals and alter Notch-dependent development in Drosophila.
abstract: In both vertebrate and invertebrate development, cells are often programmed to adopt fates distinct from their neighbors. Genetic analyses in Drosophila melanogaster have highlighted the importance of cell surface and secreted proteins in these cell fate decisions. Homologues of these proteins have been identified and shown to play similar roles in vertebrate development. Fringe, a novel signalling protein, has been shown to induce wing margin formation in Drosophila. Fringe shares significant sequence homology and predicted secondary structure similarity with bacterial glycosyltransferases. Thus fringe may control wing development by altering glycosylation of cell surface and/or secreted molecules. Recently, two fringe genes were isolated from Xenopus laevis. We report here the cloning and characterization of three murine fringe genes (lunatic fringe, manic fringe and radical fringe). We find in several tissues that fringe expression boundaries coincide with Notch-dependent patterning centres and with Notch-ligand expression boundaries. Ectopic expression of murine manic fringe or radical fringe in Drosophila results in phenotypes that resemble those seen in Notch mutants.
authors.affiliation: Division of Immunology and Cancer Research, Hospital for Sick Children, Toronto, Ontario, Canada.
authors.forename: B
authors.initials: B
authors.lastname: Cohen
authors.forename: A
authors.initials: A
authors.lastname: Bashirullah
authors.forename: L
authors.initials: L
authors.lastname: Dagnino
authors.forename: C
authors.initials: C
authors.lastname: Campbell
authors.forename: W W
authors.initials: WW
authors.lastname: Fisher
authors.forename: C C
authors.initials: CC
authors.lastname: Leow
authors.forename: E
authors.initials: E
authors.lastname: Whiting
authors.forename: D
authors.initials: D
authors.lastname: Ryan
authors.forename: D
authors.initials: D
authors.lastname: Zinyk
authors.forename: G
authors.initials: G
authors.lastname: Boulianne
authors.forename: C C
authors.initials: CC
authors.lastname: Hui
authors.forename: B
authors.initials: B
authors.lastname: Gallie
authors.forename: R A
authors.initials: RA
authors.lastname: Phillips
authors.forename: H D
authors.initials: HD
authors.lastname: Lipshitz
authors.forename: S E
authors.initials: SE
authors.lastname: Egan
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019521:Body Patterning / Q000235:genetics; D002454:Cell Differentiation; D015342:DNA Probes; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000235:genetics; D005123:Eye / Q000166:cytology; D018507:Gene Expression Regulation, Developmental / Q000235:genetics*; D005964:Glucosyltransferases; D016695:Glycosyltransferases; D017403:In Situ Hybridization; D036341:Intercellular Signaling Peptides and Proteins; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins / Q000235:genetics*; D051379:Mice; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D010641:Phenotype; D011506:Proteins / Q000235:genetics*; D051880:Receptors, Notch; D014921:Wings, Animal / Q000166:cytology; D014981:Xenopus / Q000235:genetics; D029867:Xenopus Proteins
chemical_list: D015342:DNA Probes; D029721:Drosophila Proteins; D036341:Intercellular Signaling Peptides and Proteins; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins; C497759:N protein, Drosophila; D011506:Proteins; D051880:Receptors, Notch; D029867:Xenopus Proteins; C064045:delta protein; C105140:rfng protein, Xenopus; D016695:Glycosyltransferases; D005964:Glucosyltransferases; C100015:LFNG protein, Xenopus; C498393:LFNG protein, human; C498392:Lfng protein, mouse; C486343:Mfng protein, mouse; C491317:Rfng protein, mouse; C491318:RFNG protein, human