The making of a sweet modification: structure and function of O-GlcNAc transferase.

John Janetzko, Suzanne Walker

The Journal of biological chemistry 2014 Dec 12

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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. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

Citation

John Janetzko, Suzanne Walker. The making of a sweet modification: structure and function of O-GlcNAc transferase. The Journal of biological chemistry. 2014 Dec 12;289(50):34424-32