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Molecular Interrogation to Crack the Case of O-GlcNAc.
Chemistry - A European Journal ( IF 3.9 ) Pub Date : 2020-03-23 , DOI: 10.1002/chem.202000155
Arielis Estevez 1 , Dongsheng Zhu 1 , Connor Blankenship 1 , Jiaoyang Jiang 1
Affiliation  

The O‐linked β‐N‐acetylglucosamine (O‐GlcNAc) modification, termed O‐GlcNAcylation, is an essential and dynamic post‐translational modification in cells. O‐GlcNAc transferase (OGT) installs this modification on serine and threonine residues, whereas O‐GlcNAcase (OGA) hydrolyzes it. O‐GlcNAc modifications are found on thousands of intracellular proteins involved in diverse biological processes. Dysregulation of O‐GlcNAcylation and O‐GlcNAc cycling enzymes has been detected in many diseases, including cancer, diabetes, cardiovascular and neurodegenerative diseases. Here, recent advances in the development of molecular tools to investigate OGT and OGA functions and substrate recognition are discussed. New chemical approaches to study O‐GlcNAc dynamics and its potential roles in the immune system are also highlighted. It is hoped that this minireview will encourage more research in these areas to advance the understanding of O‐GlcNAc in biology and diseases.

中文翻译:

分子探查破解 O-GlcNAc 案件。

O-连接的 β- N-乙酰氨基葡萄糖 (O-GlcNAc) 修饰,称为 O-GlcNAc 酰化,是细胞中一种重要的动态翻译后修饰。O-GlcNAc 转移酶 (OGT) 在丝氨酸和苏氨酸残基上安装这种修饰,而 O-GlcNAcase (OGA) 则将其水解。O-GlcNAc 修饰存在于参与不同生物过程的数千种细胞内蛋白质中。O-GlcNAc 酰化和 O-GlcNAc 循环酶的失调已在许多疾病中被发现,包括癌症、糖尿病、心血管和神经退行性疾病。在此,讨论了研究 OGT 和 OGA 功能以及底物识别的分子工具开发的最新进展。还强调了研究 O-GlcNAc 动力学及其在免疫系统中潜在作用的新化学方法。希望这篇小型综述能够鼓励这些领域的更多研究,以增进对 O-GlcNAc 在生物学和疾病中的理解。
更新日期:2020-03-23
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