@article{83751,
  keywords = {Animals, Rats, Recombinant Proteins, Substrate Specificity, Mice, Actins, Cytoskeleton, Fibroblasts, rho GTP-Binding Proteins, Fibronectins, Extracellular Matrix Proteins, Cell Adhesion, Tenascin, Fibrin, 3T3 Cells, GTP Phosphohydrolases, cdc42 GTP-Binding Protein},
  author = {Wenk and Midwood and Schwarzbauer},
  title = {Tenascin-C suppresses Rho activation.},
  abstract = {<p>Cell binding to extracellular matrix (ECM) components changes cytoskeletal organization by the activation of Rho family GTPases. Tenascin-C, a developmentally regulated matrix protein, modulates cellular responses to other matrix proteins, such as fibronectin (FN). Here, we report that tenascin-C markedly altered cell phenotype on a three-dimensional fibrin matrix containing FN, resulting in suppression of actin stress fibers and induction of actin-rich filopodia. This distinct morphology was associated with complete suppression of the activation of RhoA, a small GTPase that induces actin stress fiber formation. Enforced activation of RhoA circumvented the effects of tenascin. Effects of active Rho were reversed by a Rho inhibitor C3 transferase. Suppression of GTPase activation allows tenascin-C expression to act as a regulatory switch to reverse the effects of adhesive proteins on Rho function. This represents a novel paradigm for the regulation of cytoskeletal organization by ECM.</p>
},
  year = {2000},
  journal = {J Cell Biol},
  volume = {150},
  pages = {913-20},
  month = {08/2000},
  issn = {0021-9525},
  language = {eng},
}