Vimentin filament controls integrin α5β1-mediated cell adhesion by binding to integrin through its Ser38 residue

Jiyoon Kim, Jungim Jang, Chansik Yang, Eun Jin Kim, Hosung Jung, Chungho Kim

Research output: Contribution to journalLetter

4 Citations (Scopus)


Regulation of integrin affinity for its ligand is essential for cell adhesion and migration. Here, we found that direct interaction of vimentin with integrin β1 can enhance binding of integrin α5β1 to its ligand, fibronectin. Conversely, blocking the interaction reduced fibronectin binding, cell migration on a fibronectin-coated surface, and neural tube closure during Xenopus embryogenesis. We also found that withaferin A (WFA), a natural compound known to inhibit vimentin function, can suppress the vimentin–integrin interaction and abolish fibronectin binding. Finally, we identified Ser38 of vimentin as a critical residue for integrin binding. Our results suggest that phosphorylation of vimentin at Ser38 may regulate the integrin–ligand interaction, thus providing a molecular basis for antivimentin therapeutic strategies.

Original languageEnglish
Pages (from-to)3517-3525
Number of pages9
JournalFEBS Letters
Issue number20
Publication statusPublished - 2016 Oct 1



  • cell adhesion
  • integrin
  • migration
  • vimentin
  • withaferin A

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this