Glycosylation is not usually considered a "signaling" modification. However, a dynamic cycle of addition and removal of O-linked N-acetylglucosamine (O-GlcNAc) at serine and threonine residues is emerging as a key regulator of nuclear and cytoplasmic protein activity. More than a hundred proteins have been identified with this modification. Among these diverse targets are transcription factors, cytosolic enzymes, cytoskeletal proteins, and nuclear pore proteins. Like phosphorylation, this unique modification is dynamic and reversible, serving to either enhance or repress target protein activity. Most targets are also phosphoproteins, and the action of glycosylation and phosphorylation may be complementary or mutually exclusive. Whereas phosphorylation is controlled by many unique kinases and phosphatases, O-GlcNAc cycling is controlled by the efficient use of just two genes to produce differentially targeted enzymes. These enzymes are responsive to fluctuations in nutrient stores, allowing real-time control of signaling. This review will begin to answer how the enzymes of O-GlcNAc cycling are regulated and how the cycle may interface with other cellular signaling pathways.


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      signal transduction,NSDL,NSDL_SetSpec_BEN,O-linked N-acetylglucosamine,posttranslational modifications,nutrient sensor,oai:nsdl.org:2200/20080618224525338T,Life Science



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