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Structural basis of O-GlcNAc recognition by mammalian 14-3-3 proteins.

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Date
2018-06
Authors
Toleman, Clifford A
Schumacher, Maria A
Yu, Seok-Ho
Zeng, Wenjie
Cox, Nathan J
Smith, Timothy J
Soderblom, Erik J
Wands, Amberlyn M
Kohler, Jennifer J
Boyce, Michael
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Abstract
O-GlcNAc is an intracellular posttranslational modification that governs myriad cell biological processes and is dysregulated in human diseases. Despite this broad pathophysiological significance, the biochemical effects of most O-GlcNAcylation events remain uncharacterized. One prevalent hypothesis is that O-GlcNAc moieties may be recognized by "reader" proteins to effect downstream signaling. However, no general O-GlcNAc readers have been identified, leaving a considerable gap in the field. To elucidate O-GlcNAc signaling mechanisms, we devised a biochemical screen for candidate O-GlcNAc reader proteins. We identified several human proteins, including 14-3-3 isoforms, that bind O-GlcNAc directly and selectively. We demonstrate that 14-3-3 proteins bind O-GlcNAc moieties in human cells, and we present the structures of 14-3-3β/α and γ bound to glycopeptides, providing biophysical insights into O-GlcNAc-mediated protein-protein interactions. Because 14-3-3 proteins also bind to phospho-serine and phospho-threonine, they may integrate information from O-GlcNAc and O-phosphate signaling pathways to regulate numerous physiological functions.
Type
Journal article
Subject
Humans
Phosphopyruvate Hydratase
Acetylglucosamine
14-3-3 Proteins
Proteomics
Models, Molecular
Mass Spectrometry
HEK293 Cells
Permalink
https://hdl.handle.net/10161/19689
Published Version (Please cite this version)
10.1073/pnas.1722437115
Publication Info
Toleman, Clifford A; Schumacher, Maria A; Yu, Seok-Ho; Zeng, Wenjie; Cox, Nathan J; Smith, Timothy J; ... Boyce, Michael (2018). Structural basis of O-GlcNAc recognition by mammalian 14-3-3 proteins. Proceedings of the National Academy of Sciences of the United States of America, 115(23). pp. 5956-5961. 10.1073/pnas.1722437115. Retrieved from https://hdl.handle.net/10161/19689.
This is constructed from limited available data and may be imprecise. To cite this article, please review & use the official citation provided by the journal.
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Scholars@Duke

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.
Schumacher

Maria Anne Schumacher

Nanaline H. Duke Distinguished Professor of Biochemistry
Smith

Tim Smith

Student

Erik James Soderblom

Assistant Research Professor of Cell Biology
Alphabetical list of authors with Scholars@Duke profiles.
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