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MBC in Press, published online ahead of print August 29, 2007
Mol. Biol. Cell 10.1091/mbc.E07-01-0084

A more recent version of this article appeared on November 1, 2007
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Submitted on January 30, 2007
Revised on August 10, 2007
Accepted on August 17, 2007

Stable and Unstable Cadherin Dimers: Mechanisms of Formation and Roles in Cell Adhesion

Regina B. Troyanovsky,* Oscar Laur,{dagger} and Sergey M. Troyanovsky{ddagger}

*Division of Dermatology, Washington University Medical School, St. Louis, MO 63110; {dagger}Department of Pathology and Laboratory Medicine, Emory University Medical School, Atlanta, GA 30322; {ddagger}Department of Dermatology, Northwestern University, The Feinberg School of Medicine, Chicago, IL 60611

Monitoring Editor: Ben Margolis

Numerous attempts to elucidate the strength of cadherin dimerization that mediates intercellular adhesion have produced controversial and inconclusive results. To clarify this issue, we compared E-cadherin dimerization on the surface of living cells with how the same process unfolds on agarose beads. In both cases, dimerization was monitored by the same site-specific cross-linking assay, greatly simplifying data interpretation. We showed that on the agarose surface under physiological conditions, E-cadherin produced a weak dimer that immediately dissociated after the depletion of calcium ions. However, either at pH 5 or in the presence of cadmium ions, E-cadherin produced a strong dimer that was unable to dissociate upon calcium depletion. Both types of dimers were W156-dependent. Remarkably, only the strong dimer was found on the surface of living cells. We also showed that the intracellular cadherin region, the clustering of which through catenins had been proposed as stabilizer of weak intercadherin interactions, was not needed, in fact, for cadherin junction assembly. Taken together, our data present convincing evidence that cadherin adhesion is based on high-affinity cadherin-cadherin interactions.

Address correspondence to: Sergey M. Troyanovsky (sergeyt{at}im.wustl.edu)




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A. Kiss, R. B. Troyanovsky, and S. M. Troyanovsky
p120-Catenin Is a Key Component of the Cadherin-{gamma}-Secretase Supercomplex
Mol. Biol. Cell, October 1, 2008; 19(10): 4042 - 4050.
[Abstract] [Full Text] [PDF]


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