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The O-linked N-acetylglucosamine modification in cellular signalling and the immune system

The intracellular modification of proteins by the addition of a single O‐linked N ‐acetylglucosamine (O‐GlcNAc) molecule is a ubiquitous post‐translational modification in eukaryotic cells. It is catalysed by O‐linked N ‐acetylglucosaminyltransferase, which attaches O‐GlcNAc to serine/threonine resi...

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Bibliographic Details
Published in:EMBO reports 2008-08, Vol.9 (8), p.748-753
Main Authors: Golks, Alexander, Guerini, Danilo
Format: Article
Language:English
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Summary:The intracellular modification of proteins by the addition of a single O‐linked N ‐acetylglucosamine (O‐GlcNAc) molecule is a ubiquitous post‐translational modification in eukaryotic cells. It is catalysed by O‐linked N ‐acetylglucosaminyltransferase, which attaches O‐GlcNAc to serine/threonine residues, and it is counter‐regulated by β‐ N ‐acetylglucosaminidase, which is the antagonistic glycosidase that removes the O‐GlcNAc group. O‐GlcNAc modification competes with phosphorylation by protein kinases at similar sites, thereby affecting important signalling nodes. Accumulating evidence supports a central role for O‐GlcNAc modifications and the corresponding enzymes in the regulation of immune cells, particularly in the activation processes of T and B lymphocytes. Here, we discuss recent advances in the field of O‐GlcNAc modifications, focusing on the cells of the immune system.
ISSN:1469-221X
1469-3178
DOI:10.1038/embor.2008.129