Glycosylation regulates Notch signalling.
Intracellular post-translational modifications such as phosphorylation and ubiquitylation have been well studied for their roles in regulating diverse signalling pathways, but we are only just beginning to understand how differential glycosylation is used to regulate intercellular signalling. Recent studies make clear that extracellular post-translational modifications, in the form of glycosylation, are essential for the Notch signalling pathway, and that differences in the extent of glycosylation are a significant mechanism by which this pathway is regulated.
Howard Hughes Medical Institute, Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers: The State University of New Jersey, Piscataway, New Jersey 08854, USA.
Nicola
N
Haines
Kenneth D
KD
Irvine
D000818:Animals; D001683:Biological Clocks; D019521:Body Patterning; D029721:Drosophila Proteins; D004815:Epidermal Growth Factor / Q000378:metabolism; D005643:Fucose / Q000737:chemistry / Q000378:metabolism; D005647:Fucosyltransferases / Q000378:metabolism; D006031:Glycosylation; D008565:Membrane Proteins / Q000378:metabolism*; D017351:N-Acetylglucosaminyltransferases / Q000378:metabolism; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D051880:Receptors, Notch; D015398:Signal Transduction / Q000502:physiology*; D014921:Wings, Animal / Q000502:physiology
D029721:Drosophila Proteins; D008565:Membrane Proteins; D011134:Polysaccharides; D051880:Receptors, Notch; D005643:Fucose; D004815:Epidermal Growth Factor; D005647:Fucosyltransferases; D017351:N-Acetylglucosaminyltransferases; C090576:fng protein, Drosophila