O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar

被引:160
作者
Wells, L [1 ]
Hart, GW [1 ]
机构
[1] Johns Hopkins Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA
来源
FEBS LETTERS | 2003年 / 546卷 / 01期
关键词
O-GlcNAc; post-translational modification; glycosylation; phosphorylation; transcription; insulin signaling; nutrient sensing; diabetes;
D O I
10.1016/S0014-5793(03)00641-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
O-linked beta-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. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:154 / 158
页数:5
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