A Sweet Embrace: Control of Protein-Protein Interactions by O-Linked β-N-Acetylglucosamine.

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2018-01

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Abstract

O-Linked β-N-acetylglucosamine (O-GlcNAc) is a critical post-translational modification (PTM) of thousands of intracellular proteins. Reversible O-GlcNAcylation governs many aspects of cell physiology and is dysregulated in numerous human diseases. Despite this broad pathophysiological significance, major aspects of O-GlcNAc signaling remain poorly understood, including the biochemical mechanisms through which O-GlcNAc transduces information. Recent work from many laboratories, including our own, has revealed that O-GlcNAc, like other intracellular PTMs, can control its substrates' functions by inhibiting or inducing protein-protein interactions. This dynamic regulation of multiprotein complexes exerts diverse downstream signaling effects in a range of processes, cell types, and organisms. Here, we review the literature about O-GlcNAc-regulated protein-protein interactions and suggest important questions for future studies in the field.

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10.1021/acs.biochem.7b00871

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Tarbet, Heather J, Clifford A Toleman and Michael Boyce (2018). A Sweet Embrace: Control of Protein-Protein Interactions by O-Linked β-N-Acetylglucosamine. Biochemistry, 57(1). pp. 13–21. 10.1021/acs.biochem.7b00871 Retrieved from https://hdl.handle.net/10161/19692.

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Boyce

Michael Scott Boyce

Associate Professor of Biochemistry

The Boyce Lab studies mammalian cell signaling through protein glycosylation. For the latest news, project information and publications from our group, please visit our web site at http://www.boycelab.org or follow us on Twitter at https://twitter.com/BoyceLab.


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