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

dc.contributor.author

Tarbet, Heather J

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Toleman, Clifford A

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Boyce, Michael

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2020-01-01T16:57:49Z

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2020-01-01T16:57:49Z

dc.date.issued

2018-01

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2020-01-01T16:57:49Z

dc.description.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.

dc.identifier.issn

0006-2960

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1520-4995

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https://hdl.handle.net/10161/19692

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eng

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American Chemical Society (ACS)

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Biochemistry

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10.1021/acs.biochem.7b00871

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Animals

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Humans

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Acetylglucosamine

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Biochemistry

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Signal Transduction

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Protein Processing, Post-Translational

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Aminoacylation

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Models, Biological

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Protein Interaction Domains and Motifs

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Protein Multimerization

dc.title

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

dc.type

Journal article

duke.contributor.orcid

Boyce, Michael|0000-0002-2729-4876

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13

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21

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1

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School of Medicine

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Duke

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Duke Cancer Institute

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Institutes and Centers

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Biochemistry

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Basic Science Departments

pubs.publication-status

Published

pubs.volume

57

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