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Nature 446, 1017-1022 (26 April 2007) | doi:10.1038/nature05815; Published online 25 April 2007
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Cycling of O-linked 
-N-acetylglucosamine on nucleocytoplasmic proteins
Gerald W. Hart1, Michael P. Housley1 & Chad Slawson1
Abstract
All animals and plants dynamically attach and remove O-linked 
-N-acetylglucosamine (O-GlcNAc) at serine and threonine residues on myriad nuclear and cytoplasmic proteins. O-GlcNAc cycling, which is tightly regulated by the concerted actions of two highly conserved enzymes, serves as a nutrient and stress sensor. On some proteins, O-GlcNAc competes directly with phosphate for serine/threonine residues. Glycosylation with O-GlcNAc modulates signalling, and influences protein expression, degradation and trafficking. Emerging data indicate that O-GlcNAc glycosylation has a role in the aetiology of diabetes and neurodegeneration.
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