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PMID: 14570055 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Glycosylation regulates Notch signalling.

Nature reviews. Molecular cell biology ·Vol. 4 ·No. 10 ·2003-10-00 ·Pages 786-97

Haines N, Irvine KD

Abstract

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.

MeSH Terms
Animals Biological Clocks Body Patterning Drosophila Proteins Epidermal Growth Factor/metabolism Fucose/chemistry,metabolism Fucosyltransferases/metabolism Glycosylation Membrane Proteins/metabolism N-Acetylglucosaminyltransferases/metabolism Polysaccharides/chemistry,metabolism Protein Processing, Post-Translational Receptors, Notch Signal Transduction/physiology Wings, Animal/physiology
Chemicals
Drosophila Proteins Membrane Proteins Polysaccharides Receptors, Notch Fucose Epidermal Growth Factor Fucosyltransferases N-Acetylglucosaminyltransferases fng protein, Drosophila
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Haines Nicola
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.
Irvine Kenneth D
Article Info
Journal
Nature reviews. Molecular cell biology
Abbr.
Nat Rev Mol Cell Biol
ISSN
1471-0072
Published
2003-10-00
Pages
786-97
Language
English
Region
England
NLM ID
100962782
Subset
IM
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