Wells L, Vosseller K, Hart G W
Department of Biological Chemistry, Johns Hopkins School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205 USA.
Science. 2001 Mar 23;291(5512):2376-8. doi: 10.1126/science.1058714.
The dynamic glycosylation of serine or threonine residues on nuclear and cytosolic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) is abundant in all multicellular eukaryotes. On several proteins, O-GlcNAc and O-phosphate alternatively occupy the same or adjacent sites, leading to the hypothesis that one function of this saccharide is to transiently block phosphorylation. The diversity of proteins modified by O-GlcNAc implies its importance in many basic cellular and disease processes. Here we systematically examine the current data implicating O-GlcNAc as a regulatory modification important to signal transduction cascades.
在所有多细胞真核生物中，核蛋白和胞质蛋白上的丝氨酸或苏氨酸残基通过O-连接的β-N-乙酰葡糖胺（O-GlcNAc）进行的动态糖基化作用十分普遍。在几种蛋白质上，O-GlcNAc和O-磷酸交替占据相同或相邻位点，这引发了一种假说，即这种糖类的一个功能是暂时阻断磷酸化。被O-GlcNAc修饰的蛋白质的多样性暗示了其在许多基本细胞过程和疾病过程中的重要性。在此，我们系统地研究了当前表明O-GlcNAc作为对信号转导级联反应很重要的调节性修饰的相关数据。
