title: O-GlcNAc modification: a nutritional sensor that modulates proteasome function.
abstract: The addition of O-linked beta-N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a post-translational modification of nucleocytoplasmic proteins that is thought to act in a manner analogous to protein phosphorylation. Recent work shows that many proteins of the metazoan proteasome are modified by O-GlcNAc and that the level of glycosylation is responsive to the nutritional state of the cell. Moreover, increased glycosylation of the 19S (or PA700) regulatory subcomplex has been correlated with decreased proteasomal activity, suggesting a new model of proteasomal regulation.
authors.affiliation: Department of Biological Chemistry, The Johns Hopkins University Medical School, Baltimore, MD 21205-2185, USA.
authors.forename: Natasha E
authors.initials: NE
authors.lastname: Zachara
authors.forename: Gerald W
authors.initials: GW
authors.lastname: Hart
mesh_terms: D000117:Acetylglucosamine / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D004330:Drosophila / Q000201:enzymology / Q000378:metabolism; D006801:Humans; D009747:Nutritional Physiological Phenomena / Q000502:physiology*; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry* / Q000378:metabolism*; D040901:Proteomics
chemical_list: D046988:Proteasome Endopeptidase Complex; D000117:Acetylglucosamine