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

Dan P. Felsenfeld, Pamela L. Schwartzberg, Ana Venegas, Richard Tse, Michael P. Sheetz

Research output: Contribution to journalArticlepeer-review

236 Scopus citations


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 ocv but not with β1integrins. 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.

Original languageEnglish (US)
Pages (from-to)200-206
Number of pages7
JournalNature Cell Biology
Issue number4
StatePublished - Aug 1999
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology


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