| Literature DB >> 25358683 |
Karry M Jannie1, Shawn M Ellerbroek1, Dennis W Zhou2, Sophia Chen1, David J Crompton1, Andrés J García2, Kris A DeMali1.
Abstract
Vinculin binding to actin filaments is thought to be critical for force transduction within a cell, but direct experimental evidence to support this conclusion has been limited. In the present study, we found mutation (R1049E) of the vinculin tail impairs its ability to bind F-actin, stimulate actin polymerization, and bundle F-actin in vitro. Further, mutant (R1049E) vinculin expressing cells are altered in cell migration, which is accompanied by changes in cell adhesion, cell spreading and cell generation of traction forces, providing direct evidence for the critical role of vinculin in mechanotransduction at adhesion sites. Lastly, we discuss the viability of models detailing the F-actin-binding surface on vinculin in the context of our mutational analysis.Entities:
Mesh:
Substances:
Year: 2015 PMID: 25358683 PMCID: PMC4418518 DOI: 10.1042/BJ20140872
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857