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Site-specific glycosylation regulates the form and function of the intermediate filament cytoskeleton.

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Date
2018-03-07
Authors
Tarbet, Heather J
Dolat, Lee
Smith, Timothy J
Condon, Brett M
O'Brien, E Timothy
Valdivia, Raphael H
Boyce, Michael
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Abstract
Intermediate filaments (IF) are a major component of the metazoan cytoskeleton and are essential for normal cell morphology, motility, and signal transduction. Dysregulation of IFs causes a wide range of human diseases, including skin disorders, cardiomyopathies, lipodystrophy, and neuropathy. Despite this pathophysiological significance, how cells regulate IF structure, dynamics, and function remains poorly understood. Here, we show that site-specific modification of the prototypical IF protein vimentin with O-linked β-N-acetylglucosamine (O-GlcNAc) mediates its homotypic protein-protein interactions and is required in human cells for IF morphology and cell migration. In addition, we show that the intracellular pathogen Chlamydia trachomatis, which remodels the host IF cytoskeleton during infection, requires specific vimentin glycosylation sites and O-GlcNAc transferase activity to maintain its replicative niche. Our results provide new insight into the biochemical and cell biological functions of vimentin O-GlcNAcylation, and may have broad implications for our understanding of the regulation of IF proteins in general.
Type
Journal article
Subject
Cytoskeleton
Intermediate Filaments
Animals
Humans
Vimentin
N-Acetylglucosaminyltransferases
Acetylglucosamine
Signal Transduction
Cell Movement
Protein Processing, Post-Translational
Glycosylation
Phosphorylation
Permalink
https://hdl.handle.net/10161/19690
Published Version (Please cite this version)
10.7554/eLife.31807
Publication Info
Tarbet, Heather J; Dolat, Lee; Smith, Timothy J; Condon, Brett M; O'Brien, E Timothy; Valdivia, Raphael H; & Boyce, Michael (2018). Site-specific glycosylation regulates the form and function of the intermediate filament cytoskeleton. eLife, 7. 10.7554/eLife.31807. Retrieved from https://hdl.handle.net/10161/19690.
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.
Smith

Tim Smith

Student
Valdivia

Raphael H. Valdivia

Nanaline H. Duke Distinguished Professor of Molecular Genetics and Microbiology
My laboratory is interested in how microbes influence human health, both in the context of host-pathogen and host-commensal interactions.  For many pathogens, and certainly for most commensal microbes, it is is poorly understood what is the molecular basis for how host and microbial factors contribute to a beneficial outcome for us. We currently focus on two experimental systems: Chlamydia trachomatis infections are responsible for the bulk of sexually
Alphabetical list of authors with Scholars@Duke profiles.
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