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Published online 21 August 2000. doi:10.1083/jcb.150.4.913
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© The Rockefeller University Press, 0021-9525/2000//913 $5.00
The Journal of Cell Biology, Volume 150, Number 4, , 2000 913-920

Report

Tenascin-C Suppresses Rho Activation



Melissa B. Wenka, Kim S. Midwooda, and Jean E. Schwarzbauera

a Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014
Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014.(609) 258-1035(609) 258-2893

jschwarzbauer{at}molbio.princeton.edu

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.

Key Words: tenascin-C • provisional matrix • fibronectin • Rho GTPase • filopodia

© 2000 The Rockefeller University Press

Abbreviations used in this paper: ECM, extracellular matrix; 70Ten, recombinant chimeric protein containing FN and tenascin-C sequences; FN, fibronectin; RGD, arginine-glycine-aspartic acid cell-binding sequence.


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