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A Sweet Embrace: Control of Protein–Protein Interactions by O-Linked β-N-Acetylglucosamine
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    A Sweet Embrace: Control of Protein–Protein Interactions by O-Linked β-N-Acetylglucosamine
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    Department of Biochemistry, Duke University School of Medicine, Durham, North Carolina 27710, United States
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    Biochemistry

    Cite this: Biochemistry 2018, 57, 1, 13–21
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    https://doi.org/10.1021/acs.biochem.7b00871
    Published November 3, 2017
    Copyright © 2017 American Chemical Society

    Abstract

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    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.

    Copyright © 2017 American Chemical Society

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    Cited By

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    This article is cited by 32 publications.

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    Biochemistry

    Cite this: Biochemistry 2018, 57, 1, 13–21
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.biochem.7b00871
    Published November 3, 2017
    Copyright © 2017 American Chemical Society

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