Selective regulation of integrin–cytoskeleton interactions by the tyrosine kinase Src

Abstract

Cell motility on extracellular-matrix (ECM) substrates depends on the regulated generation of force against the substrate through adhesion receptors known as integrins. Here we show that integrin-mediated traction forces can be selectively modulated by the tyrosine kinase Src. In Src-deficient fibroblasts, cell spreading on the ECM component vitronectin is inhibited, while the strengthening of linkages between integrin vitronectin receptors and the force-generating cytoskeleton in response to substrate rigidity is dramatically increased. In contrast, Src deficiency has no detectable effects on fibronectin-receptor function. Finally, truncated Src (lacking the kinase domain) co-localizes to focal-adhesion sites with αv but not with β1 integrins. These data are consistent with a selective, functional interaction between Src and the vitronectin receptor that acts at the integrin–cytoskeleton interface to regulate cell spreading and migration.

Cite this article

Felsenfeld, D., Schwartzberg, P., Venegas, A. et al. Selective regulation of integrin–cytoskeleton interactions by the tyrosine kinase Src. Nat Cell Biol 1, 200–206 (1999). https://doi.org/10.1038/12021

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