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Published online
doi:10.1083/jcb.200701058
The Journal of Cell Biology, Vol. 178, No. 3, 517-527
The Rockefeller University Press, 0021-9525 $30.00
© Yamada et al.
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Article

Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell–cell adhesion



Soichiro Yamada1 and W. James Nelson1,2

1 Department of Molecular and Cellular Physiology and 2 Department of Biological Sciences, Stanford University, Stanford, CA 94305

Correspondence to W. James Nelson: wjnelson{at}stanford.edu

Spatiotemporal coordination of cell–cell adhesion involving lamellipodial interactions, cadherin engagement, and the lateral expansion of the contact is poorly understood. Using high-resolution live-cell imaging, biosensors, and small molecule inhibitors, we investigate how Rac1 and RhoA regulate actin dynamics during de novo contact formation between pairs of epithelial cells. Active Rac1, the Arp2/3 complex, and lamellipodia are initially localized to de novo contacts but rapidly diminish as E-cadherin accumulates; further rounds of activation and down-regulation of Rac1 and Arp2/3 occur at the contacting membrane periphery, and this cycle repeats as a restricted membrane zone that moves outward with the expanding contact. The cortical bundle of actin filaments dissolves beneath the expanding contacts, leaving actin bundles at the contact edges. RhoA and actomyosin contractility are activated at the contact edges and are required to drive expansion and completion of cell–cell adhesion. We show that zones of Rac1 and lamellipodia activity and of RhoA and actomyosin contractility are restricted to the periphery of contacting membranes and together drive initiation, expansion, and completion of cell–cell adhesion.

S. Yamada's present address is Department of Biomedical Engineering, Genome and Biomedical Sciences Facility, University of California, Davis, Davis, CA 95616.

Abbreviations used in this paper: CD, cytochalasin D; FRET, fluorescence resonance energy transfer; MLCK, myosin light chain kinase; ROCK, Rho kinase; TIRF-M, total internal reflection fluorescence microscopy.


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