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

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Tarbet, HJ; Dolat, L; Smith, TJ; Condon, BM; O'Brien, ET; Valdivia, RH; Boyce, M

Published Date

  • March 7, 2018

Published In

Volume / Issue

  • 7 /

PubMed ID

  • 29513221

Pubmed Central ID

  • PMC5841932

Electronic International Standard Serial Number (EISSN)

  • 2050-084X

Digital Object Identifier (DOI)

  • 10.7554/eLife.31807


  • eng

Conference Location

  • England