Vosseller Keith, Sakabe Kaoru, Wells Lance, Hart Gerald W
Johns Hopkins University School of Medicine, Department of Biological Chemistry, Baltimore, MD 21218, USA.
Curr Opin Chem Biol. 2002 Dec;6(6):851-7. doi: 10.1016/s1367-5931(02)00384-8.
N-Acetylglucosamine O-linked to serines and threonines of cytosolic and nuclear proteins (O-GlcNAc) is an abundant reversible post-translational modification found in all higher eukaryotes. Evidence for functional regulation of proteins by this dynamic saccharide is rapidly accumulating. Deletion of the gene encoding the enzyme that attaches O-GlcNAc (OGT) is lethal at the single cell level, indicating the fundamental requirement for this modification. Recent studies demonstrate a role for O-GlcNAcylation in processes as diverse as transcription in the nucleus and signaling in the cytoplasm, suggesting that O-GlcNAc has both protein and site-specific influences on biochemistry and metabolism throughout the cell.
与胞质和核蛋白的丝氨酸及苏氨酸相连的N-乙酰葡糖胺（O-连接的N-乙酰葡糖胺，O-GlcNAc）是在所有高等真核生物中都存在的一种丰富的可逆翻译后修饰。这种动态糖类对蛋白质进行功能调控的证据正在迅速积累。编码连接O-GlcNAc的酶（OGT）的基因缺失在单细胞水平是致死的，这表明这种修饰是基本必需的。最近的研究表明，O-GlcNAc糖基化在细胞核转录和细胞质信号传导等多种过程中发挥作用，这表明O-GlcNAc对整个细胞的生物化学和代谢具有蛋白质特异性及位点特异性的影响。
