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EMBO reports 9, 8, 748–753 (2008)
doi:10.1038/embor.2008.129
AOP Published online: 11 July 2008
The O-linked N-acetylglucosamine modification in cellular signalling and the immune system. 'Protein Modifications: Beyond the Usual Suspects' Review Series
Alexander Golks & Danilo Guerini
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Autoimmunity, Transplantation and Inflammation, Novartis Pharma AG, Forum 1, Novartis Campus, Basel CH-4056, Switzerland
To whom correspondence should be addressed
Danilo Guerini Tel: +41 61 3243862; Fax: +41 61 3242488;
E-mail: danilo.guerini@novartis.com
Received 18 March 2008; Accepted 10 June 2008; Published online 11 July 2008.
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Abstract
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  -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.
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