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The O-linked N-acetylglucosamine modification in cellular signalling and the immune system. ‘Protein Modifications: Beyond the Usual Suspects' Review Series

机译:在细胞信号转导和免疫系统中进行O-连接的N-乙酰氨基葡萄糖修饰。 “蛋白质修饰:超越常规嫌疑人”系列

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摘要

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.
机译:通过添加单个O-连接的N-乙酰氨基葡萄糖(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-乙酰氨基葡萄糖氨基转移酶催化,该酶将O-GlcNAc连接到丝氨酸/苏氨酸残基上,并受到β-N-乙酰氨基葡萄糖氨基转移酶的调控,β-N-乙酰氨基葡糖苷酶是去除O-GlcNAc基团的拮抗糖苷酶。 O-GlcNAc修饰与蛋白激酶在类似位点的磷酸化竞争,从而影响重要的信号传导节点。越来越多的证据支持O-GlcNAc修饰和相应的酶在调节免疫细胞,特别是在T和B淋巴细胞的激活过程中起着核心作用。在这里,我们讨论O-GlcNAc修饰领域的最新进展,重点是免疫系统的细胞。

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