The post-translational modification of proteins by O-linked N-acetylglucosamine (O-GlcNAc) dynamically programmes cellular physiology to maintain homoeostasis and tailor biochemical pathways to meet context-dependent cellular needs. Despite diverse roles of played by O-GlcNAc, only two enzymes act antagonistically to govern its cycling; O-GlcNAc transferase installs the monosaccharide on target proteins, and O-GlcNAc hydrolase removes it. The recent literature has exposed a network of mechanisms regulating these two enzymes to choreograph global, and target-specific, O-GlcNAc cycling in response to cellular stress and nutrient availability. Herein, we amalgamate these emerging mechanisms from a structural and molecular perspective to explore how the cell exerts fine control to regulate O-GlcNAcylation of diverse proteins in a selective fashion.

中文翻译：

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调节O-连接的N-乙酰氨基葡萄糖（O-GlcNAc）加工酶的分子机制。

通过O-连接的N-乙酰氨基葡萄糖（O-GlcNAc）对蛋白质进行翻译后修饰，可以动态地编程细胞生理学，以维持同源性并调整生化途径，以满足上下文相关的细胞需求。尽管O-GlcNAc发挥着不同的作用，但只有两种酶起拮抗作用来控制其循环。O-GlcNAc转移酶将单糖安装在目标蛋白上，O-GlcNAc水解酶将其去除。最近的文献已经揭示了调节这两种酶的机制网络，以响应于细胞应激和营养物质的利用而在编舞全局的和靶标特异性的O-GlcNAc循环中发挥作用。在这里，我们从结构和分子的角度融合这些新兴的机制，以探索细胞如何发挥精细控制作用，以选择性方式调节多种蛋白质的O-GlcNAcy酰化。