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.
Bibliographical noteFunding Information:
This work was supported by a grant from the Korea Healthcare Technology R&D Project, Ministry of Health and Welfare, Republic of Korea [grant number HI14C0209], and by a Korea University Grant.
© 2016 Federation of European Biochemical Societies
- cell adhesion
- withaferin A
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
- Cell Biology