O'Donnell Niall
Department of Cellular and Molecular Medicine, The Howard Hughes Medical Institute, Glycobiology Research and Training Center, University of California San Diego, La Jolla 92093, USA.
Biochim Biophys Acta. 2002 Dec 19;1573(3):336-45. doi: 10.1016/s0304-4165(02)00401-4.
O-linked N-acetylglucosamine (O-GlcNAc) is a highly dynamic post-translational modification of cytoplasmic and nuclear proteins. Although the function of this abundant modification is yet to be definitively elucidated, all O-GlcNAc proteins are phosphoproteins. Further, the serine and threonine residues substituted with O-GlcNAc are often sites of, or close to sites of, protein phosphorylation. This implies that there may be a dynamic interplay between these two post-translational modifications to regulate protein function. In this review, the functions of some of the proteins that are modified by O-GlcNAc will be considered in the context of the potential role of the O-GlcNAc modification. Furthermore, predictions will be made as to how cellular function and developmental regulation might be affected by changes in O-GlcNAc levels.
O-连接的N-乙酰葡糖胺（O-GlcNAc）是一种对细胞质和细胞核蛋白进行的高度动态的翻译后修饰。尽管这种丰富修饰的功能尚未得到明确阐明，但所有O-GlcNAc化蛋白都是磷蛋白。此外，被O-GlcNAc取代的丝氨酸和苏氨酸残基通常是蛋白磷酸化的位点或靠近蛋白磷酸化的位点。这意味着这两种翻译后修饰之间可能存在动态相互作用以调节蛋白功能。在本综述中，将在O-GlcNAc修饰的潜在作用背景下考虑一些被O-GlcNAc修饰的蛋白的功能。此外，还将预测O-GlcNAc水平的变化可能如何影响细胞功能和发育调控。
