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First published online 4 March 2003
doi: 10.1242/jcs.00340
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Research Article |
1 Department of Biochemistry and Molecular Biophysics, Washington University
School of Medicine, St Louis, MO 63110, USA
2 Department of Pathology and Anesthesiology, St Louis University School of
Medicine, St Louis, MO 63104, USA
* Author for correspondence (e-mail: elson{at}biochem.wustl.edu)
Accepted 2 January 2003
As it migrates over a substratum, a cell must exert different kinds of forces that act at various cellular locations and at specific times. These forces must therefore be coordinately regulated. The Rho-family GTPases Rac1 and Cdc42 promote actin polymerization that drives extension of the leading cell edge. Subsequently, RhoA regulates myosin-dependent contractile force, which is required for formation of adhesive contacts and stress fibers. During cell spreading, however, the activity of RhoA is reduced by a mechanism involving the tyrosine kinases c-Src and focal adhesion kinase (FAK), and the p190RhoGAP. It has been proposed that this reduction of RhoA activity facilitates edge extension by reducing myosin-dependent contractile forces that could resist this process. We have directly tested this hypothesis by correlating myosin activity with the rate of cell spreading on a substratum. The rate of spreading is inversely related to the myosin activity. Furthermore, spreading is inhibited by low concentrations of cytochalasin D, as expected for a process that depends on the growth of uncapped actin filaments. Cell indentation measurements show that a myosin-dependent viscoelastic force resists cell deformation.
Key words: Myosin II, Cell spreading, Cell mechanics, Traction force, Contraction, Cytochalasin D
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