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

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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 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.