Tenascin-C suppresses Rho activation

M. B. Wenk, K. S. Midwood, J. E. Schwarzbauer

Research output: Contribution to journalArticlepeer-review

111 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)913-919
Number of pages7
JournalJournal of Cell Biology
Issue number4
StatePublished - Aug 21 2000

All Science Journal Classification (ASJC) codes

  • Cell Biology


  • Fibronectin
  • Filopodia
  • Provisional matrix
  • Rho GTPase
  • Tenascin-C


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