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The O‐linked N ‐acetylglucosamine modification in cellular signalling and the immune system
Author(s) -
Golks Alexander,
Guerini Danilo
Publication year - 2008
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2008.129
Subject(s) - phosphorylation , threonine , serine , kinase , immune system , n acetylglucosamine , microbiology and biotechnology , biochemistry , enzyme , chemistry , intracellular , glycosylation , posttranslational modification , biology , genetics
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.