Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins.
All animals and plants dynamically attach and remove O-linked beta-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.
Hart
Gerald W
GW
Department of Biological Chemistry, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205-2185, USA. gwhart@jhmi.edu
Housley
Michael P
MP
Slawson
Chad
C
D000117:Acetylglucosamine / Q000031:analogs & derivatives / Q000737:chemistry* / Q000378:metabolism*; D000544:Alzheimer Disease / Q000378:metabolism; D000818:Animals; D003593:Cytoplasm / Q000737:chemistry / Q000378:metabolism*; D004798:Enzymes / Q000378:metabolism; D006801:Humans; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism
D004798:Enzymes; D009687:Nuclear Proteins; D010710:Phosphates; D000117:Acetylglucosamine