Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
Curr Opin Chem Biol. 2013 Oct;17(5):719-28. doi: 10.1016/j.cbpa.2013.06.030. Epub 2013 Jul 30.
Intracellular glycosylation of nuclear and cytoplasmic proteins involves the addition of N-acetylglucosamine (O-GlcNAc) to serine and threonine residues. This dynamic modification occurs on hundreds of proteins and is involved in various essential biological processes. Because O-GlcNAc is substoichiometric and labile, identifying proteins and sites of modification has been challenging and generally requires proteome enrichment. Here we review recent advances on the implementation of chemical tools to perturb, to detect, and to map O-GlcNAc in living systems. Metabolic and chemoenzymatic labels along with bioorthogonal reactions and quantitative proteomics are enabling investigation of the role of O-GlcNAc in various processes including transcriptional regulation, neurodegeneration, and cell signaling.
细胞内核蛋白和细胞质蛋白的糖基化涉及到将 N-乙酰葡萄糖胺（O-GlcNAc）添加到丝氨酸和苏氨酸残基上。这种动态修饰发生在数百种蛋白质上，参与了各种重要的生物学过程。由于 O-GlcNAc 的亚化学计量和不稳定性，鉴定蛋白质和修饰位点一直具有挑战性，通常需要进行蛋白质组富集。在这里，我们综述了化学工具在活细胞中干扰、检测和绘制 O-GlcNAc 方面的最新进展。代谢和化学酶标记物以及生物正交反应和定量蛋白质组学正在使 O-GlcNAc 在包括转录调控、神经退行性变和细胞信号转导在内的各种过程中的作用的研究成为可能。
