*Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, DD1 5EH, U.K.
Biochem J. 2013 Nov 15;456(1):1-12. doi: 10.1042/BJ20131081.
Protein O-GlcNAcylation is an abundant, dynamic and reversible type of protein post-translational modification in animals that has been implicated in signalling processes linked to innate immunity, stress response, growth factor response, transcription, translation and proteosomal degradation. Only two enzymes, O-GlcNAc (O-linked N-acetylglucosamine) transferase and O-GlcNAcase, catalyse the reversible addition of the O-GlcNAc residue to over 1000 target proteins in the human cell. Recent advances in our understanding of the structures and mechanisms of these enzymes have resulted in the development of potent and selective inhibitors. The present review gives an overview of these inhibitors and how they have been used on cell lines, primary cells and animals to modulate O-GlcNAc levels and study the effects on signal transduction.
蛋白质 O-GlcNAc 糖基化是一种在动物中广泛存在、动态可逆的蛋白质翻译后修饰方式，与先天免疫、应激反应、生长因子反应、转录、翻译和蛋白酶体降解等信号过程有关。只有两种酶，O-GlcNAc（O-连接 N-乙酰葡萄糖胺）转移酶和 O-GlcNAcase，能够催化 O-GlcNAc 残基可逆地添加到人类细胞中的 1000 多个靶蛋白上。我们对这些酶的结构和机制的理解的最新进展，导致了有效和选择性抑制剂的发展。本综述概述了这些抑制剂，以及它们如何在细胞系、原代细胞和动物中被用来调节 O-GlcNAc 水平，并研究对信号转导的影响。
