Wells Lance, Hart Gerald W
Johns Hopkins School of Medicine, Department of Biological Chemistry, 725 N. Wolfe St., Baltimore, MD 21205, USA.
FEBS Lett. 2003 Jul 3;546(1):154-8. doi: 10.1016/s0014-5793(03)00641-0.
O-linked beta-N-acetylglucosamine (O-GlcNAc) is a dynamic nucleocytoplasmic post-translational modification more analogous to phosphorylation than to classical complex O-glycosylation. A large number of nuclear and cytosolic proteins are modified by O-GlcNAc. Proteins modified by O-GlcNAc include transcription factors, signaling components, and metabolic enzymes. While the modification has been known for almost 20 years, functions for the monosaccharide modification are just now emerging. In this review, we will focus on the cycling enzymes and emerging roles for this post-translational modification in regulating signal transduction and transcription. Finally, we will discuss future directions and the working model of O-GlcNAc serving as a nutrient sensor.
O-连接的β-N-乙酰葡糖胺（O-GlcNAc）是一种动态的核质翻译后修饰，与磷酸化的相似性高于经典的复杂O-糖基化。大量的核蛋白和胞质蛋白都被O-GlcNAc修饰。被O-GlcNAc修饰的蛋白质包括转录因子、信号转导成分和代谢酶。虽然这种修饰已被知晓近20年，但这种单糖修饰的功能才刚刚显现出来。在这篇综述中，我们将聚焦于循环酶以及这种翻译后修饰在调节信号转导和转录方面新出现的作用。最后，我们将讨论未来的方向以及O-GlcNAc作为营养传感器的工作模式。
