4.5 Review

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

Journal

FEBS LETTERS
Volume 546, Issue 1, Pages 154-158

Publisher

WILEY
DOI: 10.1016/S0014-5793(03)00641-0

Keywords

O-GlcNAc; post-translational modification; glycosylation; phosphorylation; transcription; insulin signaling; nutrient sensing; diabetes

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available