O-GlcNAc Modification of the Extracellular Domain of Notch Receptors

Epidermal growth factor (EGF) domains are posttranslationally modified with unique O-linked glycans. The classical types of O-glycans on EGF domains are O-fucose and O-glucose glycans, found on many plasma glycoproteins and signaling molecules, whose biological functions have been demonstrated espec...

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Bibliographic Details
Published in:Trends in Glycoscience and Glycotechnology 2010, Vol.22(127), pp.247-255
Main Authors: Okajima, Tetsuya, Furukawa, Koichi, Sakaidani, Yuta
Format: Article
Language:eng ; jpn
Subjects:
EGF domain
Notch
O-GlcNAc
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Summary:Epidermal growth factor (EGF) domains are posttranslationally modified with unique O-linked glycans. The classical types of O-glycans on EGF domains are O-fucose and O-glucose glycans, found on many plasma glycoproteins and signaling molecules, whose biological functions have been demonstrated especially in the context of the Notch signaling pathway. We recently discovered O-GlcNAc modification as a new modification of the EGF domain that occurs on the conserved Ser/Thr residue located between the fifth and sixth cysteine residues within the EGF domains of Notch receptors in Drosophila. Isolation of the unidentified enzyme responsible for the extracellular O-GlcNAcylation and characterization of the O-GlcNAc transferase gene will reveal the new biological roles for O-GlcNAcylation in secreted and membrane glycoproteins and the extracellular environment.
ISSN:0915-7352
1883-2113
DOI:10.4052/tigg.22.247