| Literature DB >> 25336649 |
John Janetzko1, Suzanne Walker2.
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.Entities:
Keywords: Crystal Structure; Enzymology; Glycosylation; Glycosyltransferase; Host Cell Factor 1; Ligand-binding Protein; O-GlcNAcylation
Mesh:
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Year: 2014 PMID: 25336649 PMCID: PMC4263849 DOI: 10.1074/jbc.R114.604405
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157