title: The making of a sweet modification: structure and function of O-GlcNAc transferase.
abstract: O-GlcNAc transferase is an essential mammalian enzyme responsible for transferring a single GlcNAc moiety from UDP-GlcNAc to specific serine/threonine residues of hundreds of nuclear and cytoplasmic proteins. This modification is dynamic and has been implicated in numerous signaling pathways. An unexpected second function for O-GlcNAc transferase as a protease involved in cleaving the epigenetic regulator HCF-1 has also been reported. Recent structural and biochemical studies that provide insight into the mechanism of glycosylation and HCF-1 cleavage will be described, with outstanding questions highlighted.
authors.affiliation: the Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138.
authors.forename: John
authors.initials: J
authors.lastname: Janetzko
authors.affiliation: From the Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts 02115 and suzanne_walker@hms.harvard.edu.
authors.forename: Suzanne
authors.initials: S
authors.lastname: Walker
mesh_terms: D000818:Animals; D006031:Glycosylation; D051863:Host Cell Factor C1 / Q000378:metabolism; D006801:Humans; D017351:N-Acetylglucosaminyltransferases / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D059748:Proteolysis
chemical_list: D051863:Host Cell Factor C1; D017351:N-Acetylglucosaminyltransferases; C449880:O-GlcNAc transferase
keywords: Crystal Structure; Enzymology; Glycosylation; Glycosyltransferase; Host Cell Factor 1; Ligand-binding Protein; O-GlcNAcylation