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Selective regulation of integrin–cytoskeleton interactions by the tyrosine kinase Src
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Journal Article
Selective regulation of integrin–cytoskeleton interactions by the tyrosine kinase Src
1999
Overview
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 α
v
but not with β
1
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.
Publisher
Nature Publishing Group UK
Subject
/ Biomedical and Life Sciences
/ Luminescent Proteins - genetics
/ Luminescent Proteins - metabolism
/ Mice
/ Receptors, Fibronectin - metabolism
/ Receptors, Vitronectin - metabolism
/ Recombinant Fusion Proteins - genetics
/ Recombinant Fusion Proteins - metabolism
/ src-Family Kinases - genetics
