Golks Alexander, Guerini Danilo
Autoimmunity, Transplantation and Inflammation, Novartis Pharma AG, Forum 1, Novartis Campus, Basel CH-4056, Switzerland.
EMBO Rep. 2008 Aug;9(8):748-53. doi: 10.1038/embor.2008.129. Epub 2008 Jul 11.
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.
通过添加单个O-连接的N-乙酰葡糖胺（O-GlcNAc）分子对蛋白质进行的细胞内修饰是真核细胞中普遍存在的翻译后修饰。它由O-连接的N-乙酰葡糖胺基转移酶催化，该酶将O-GlcNAc连接到丝氨酸/苏氨酸残基上，并且由β-N-乙酰葡糖胺酶进行反向调节，β-N-乙酰葡糖胺酶是去除O-GlcNAc基团的拮抗糖苷酶。O-GlcNAc修饰在相似位点与蛋白激酶的磷酸化相互竞争，从而影响重要的信号节点。越来越多的证据支持O-GlcNAc修饰及相应酶在免疫细胞调节中，特别是在T和B淋巴细胞的激活过程中发挥核心作用。在此，我们讨论O-GlcNAc修饰领域的最新进展，重点关注免疫系统的细胞。
