The O-linked N-acetylglucosamine modification in cellular signalling and the immune system. 'Protein modifications: beyond the usual suspects' review series.
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 beta-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.
Golks
Alexander
A
Autoimmunity, Transplantation and Inflammation, Novartis Pharma AG, Forum 1, Novartis Campus, Basel CH-4056, Switzerland.
Guerini
Danilo
D
D000117:Acetylglucosamine / Q000737:chemistry / Q000378:metabolism*; D000118:Acetylglucosaminidase / Q000378:metabolism; D007107:Immune System / Q000378:metabolism*; D008954:Models, Biological; D017351:N-Acetylglucosaminyltransferases / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction / Q000502:physiology*
D017351:N-Acetylglucosaminyltransferases; D000118:Acetylglucosaminidase; D000117:Acetylglucosamine