O‐GlcNAc turns twenty: functional implications for post‐translational modification of nuclear and cytosolic proteins with a sugar
O‐GlcNAc turns twenty: functional implications for post‐translational modification of nuclear and cytosolic proteins with a sugar
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DOI：
10.1016/s0014-5793(03)00641-0
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发表时间：
2003-07
期刊：
影响因子：
3.5
通讯作者：
L. Wells;G. Hart
中科院分区：
文献类型：
--
作者：
L. Wells;G. Hart
O-连接的β-N-乙酰葡萄糖胺（O-GlcNAc）是一种动态的核质翻译后修饰，与经典的复杂O-糖基化相比，更类似于磷酸化。O-GlcNAc修饰了大量的核蛋白和胞浆蛋白。O-GlcNAc修饰的蛋白质包括转录因子、信号传导组分和代谢酶。虽然修饰已经知道了近20年，单糖修饰的功能才刚刚出现。在这篇综述中，我们将集中在循环酶和新出现的作用，这种翻译后修饰在调节信号转导和转录。最后，我们将讨论未来的发展方向和O-GlcNAc作为营养传感器的工作模式。
O-linked β-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.