Site-specific glycosylation regulates the form and function of the intermediate filament cytoskeleton.
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 articleSubject
CytoskeletonIntermediate Filaments
Animals
Humans
Vimentin
N-Acetylglucosaminyltransferases
Acetylglucosamine
Signal Transduction
Cell Movement
Protein Processing, Post-Translational
Glycosylation
Phosphorylation
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https://hdl.handle.net/10161/19690Published Version (Please cite this version)
10.7554/eLife.31807Publication 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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Show full item recordScholars@Duke
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.
Tim Smith
Student
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
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