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O‐GlcNAc turns twenty: functional implications for post‐translational modification of nuclear and cytosolic proteins with a sugar
Author(s) -
Wells Lance,
Hart Gerald W.
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00641-0
Subject(s) - cytosol , posttranslational modification , glycosylation , phosphorylation , signal transduction , chemistry , biochemistry , nutrient sensing , transcription (linguistics) , enzyme , transcription factor , microbiology and biotechnology , biology , gene , linguistics , philosophy
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.