Regulation of signal transduction pathways in development by glycosylation.
Recent studies from several laboratories have provided evidence that cell surface complex carbohydrates play key roles in the regulation of developmentally relevant signal transduction events. The demonstration that Fringe, a known modifier of Notch function, is a fucose-specific N-acetylglucosaminyltransferase provided strong evidence that the Notch signaling pathway could be regulated by alterations of O-fucose structures. More recently, the demonstration that O-fucose modification of Cripto is essential for Nodal-dependent signaling provides further evidence of a role for glycosylation in signal transduction. These and other examples provide a new paradigm for the regulation of signal transduction events by glycosylation.
Haltiwanger
Robert S
RS
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York at Stony Brook, Stony Brook, NY 11794-5215, USA.
D000818:Animals; D002240:Carbohydrate Sequence; D002462:Cell Membrane / Q000502:physiology*; D029721:Drosophila Proteins / Q000502:physiology; D005643:Fucose / Q000378:metabolism; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D008565:Membrane Proteins / Q000502:physiology; D008969:Molecular Sequence Data; D017351:N-Acetylglucosaminyltransferases / Q000502:physiology; D009844:Oligosaccharides / Q000737:chemistry; D051880:Receptors, Notch; D015398:Signal Transduction / Q000502:physiology*
D029721:Drosophila Proteins; D006023:Glycoproteins; D008565:Membrane Proteins; D009844:Oligosaccharides; D051880:Receptors, Notch; D005643:Fucose; D017351:N-Acetylglucosaminyltransferases; C090576:fng protein, Drosophila