Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins

Gerald W. Hart (), Michael P. Housley and Chad Slawson
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Gerald W. Hart: Johns Hopkins University, School of Medicine
Michael P. Housley: Johns Hopkins University, School of Medicine
Chad Slawson: Johns Hopkins University, School of Medicine

Nature, 2007, vol. 446, issue 7139, 1017-1022

Abstract: Abstract All animals and plants dynamically attach and remove O-linked β-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.

Date: 2007
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DOI: 10.1038/nature05815

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