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

FEBS Letters

Hart, Gerald W.¹  Wells, Lance¹ 

[1] Johns Hopkins School of Medicine, Department of Biological Chemistry, 725 N. Wolfe St., Baltimore, MD 21205, USA

关键词: O-GlcNAc;    Post-translational modification;    Glycosylation;    Phosphorylation;    Transcription;    Insulin signaling;    Nutrient sensing;    Diabetes;   

DOI  :  10.1016/S0014-5793(03)00641-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

O-linked β-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.

【 授权许可】

Unknown