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Vol. 12, Issue 2, 265-277, February 2001
and
*Departments of Pediatrics and Pharmacology, University of
Wisconsin, Madison, Wisconsin 53706; and Integrin-mediated adhesion is a critical regulator of cell
migration. Here we demonstrate that integrin-mediated adhesion to high fibronectin concentrations induces a stop signal for cell migration by inhibiting cell polarization and protrusion. On
fibronectin, the stop signal is generated through Department of
Cell Biology and Anatomy, University of North Carolina, Chapel Hill,
North Carolina 27599
5
1
integrin-mediated signaling to the Rho family of GTPases.
Specifically, Cdc42 and Rac1 activation exhibits a biphasic dependence
on fibronectin concentration that parallels optimum cell polarization
and protrusion. In contrast, RhoA activity increases with increasing
substratum concentration. We find that cross talk between Cdc42 and
Rac1 is required for substratum-stimulated protrusion, whereas RhoA
activity is inhibitory. We also show that Cdc42 activity is inhibited
by Rac1 activation, suggesting that Rac1 activity may down-regulate
Cdc42 activity and promote the formation of stabilized rather than
transient protrusion. Furthermore, expression of RhoA down-regulates
Cdc42 and Rac1 activity, providing a mechanism whereby RhoA may inhibit cell polarization and protrusion. These findings implicate
adhesion-dependent signaling as a mechanism to stop cell migration by
regulating cell polarity and protrusion via the Rho family of GTPases.
Online version of this article contains video
material for Figure 1. The online version is available at
www.molbiolcell.org.
Corresponding author. E-mail address:
huttenlocher{at}facstaff.wisc.edu.
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