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Vol. 16, Issue 10, 4531-4542, October 2005
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* Division of Molecular Cell Biology, Institute for Molecular Bioscience;
School for Biomedical Science, The University of Queensland, St. Lucia, Queensland 4072, Australia
Submitted April 21, 2005;
Accepted July 12, 2005
Monitoring Editor: Martin A. Schwartz
Classical cadherins accumulate at cell–cell contacts as a characteristic response to productive adhesive ligation. Such local accumulation of cadherins is a developmentally regulated process that supports cell adhesiveness and cell–cell cohesion. Yet the molecular effectors responsible for cadherin accumulation remain incompletely understood. We now report that Myosin 2 is critical for cells to concentrate E-cadherin at cell–cell contacts. Myosin 2 is found at cadherin-based cell–cell contacts and its recruitment requires E-cadherin activity. Indeed, both Myosin 2 recruitment and its activation were stimulated by E-cadherin homophilic ligation alone. Inhibition of Myosin 2 activity by blebbistatin or ML-7 rapidly impaired the ability of cells to concentrate E-cadherin at adhesive contacts, accompanied by decreased cadherin-based cell adhesiveness. The total surface expression of cadherins was unaffected, suggesting that Myosin 2 principally regulates the regional distribution of cadherins at the cell surface. The recruitment of Myosin 2 to cadherin contacts, and its activation, required Rho kinase; furthermore, inhibition of Rho kinase signaling effectively phenocopied the effects of Myosin 2 inhibition. We propose that Myosin 2 is a key effector of Rho-Rho kinase signaling that regulates cell–cell adhesion by determining the ability of cells to concentrate cadherins at contacts in response to homophilic ligation.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
Address correspondence to: Alpha S. Yap (a.yap{at}imb.uq.edu.au).
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