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Papers In Press, published online ahead of print July 16, 2001
J. Biol. Chem, 10.1074/jbc.C100306200
Submitted on June 7, 2001
Revised on July 10, 2001
Accepted on July 16, 2001
Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7090
Corresponding Author: Nicole_Noren{at}med.unc.edu
The formation of cell-cell adherens junctions is a cadherin-mediated process associated with reorganization of the actin cytoskeleton. Since Rho family GTPases regulate actin dynamics, we have investigated whether cadherin-mediated adhesion regulates the activity of RhoA, Rac1 and Cdc42. Confluent epithelial cells were found to have elevated Rac1 and Cdc42 activity, but decreased RhoA activity, when compared to low density cultures. Using a calcium switch method to manipulate junction assembly, we found that induction of cell-cell junctions increased Rac1 activity, and this was inhibited by E-cadherin function-blocking antibodies. Using the same calcium switch procedure, there was little effect on RhoA activity during the first hour of junction assembly. However, over several hours, RhoA activity significantly decreased. To determine if these effects are directly mediated through cadherins or indirectly through engagement of other surface proteins downstream from junction assembly, we have used a model system in which cadherin engagement is induced without cell-cell contact. For these experiments, CHO cells expressing C-cadherin were plated on the extracellular domain of C-cadherin immobilized on tissue culture plates. Whereas, direct cadherin engagement did not stimulate Cdc42 activity, it strongly inhibited RhoA activity, but increased Rac1 activity. Deletion of the C-cadherin cytoplasmic domain abolished these effects.
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