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© The Rockefeller University Press, 0021-9525/1998//837 $5.00
The Journal of Cell Biology, Volume 142, Number 3, , 1998 837-846

Regular Articles

Adhesive But Not Lateral E-cadherin Complexes Require Calcium and Catenins for Their Formation



Nikolai A. Chitaev{dagger} and Sergey M. Troyanovsky

Department of Dermatology, Washington University Medical School, St. Louis, Missouri 63110

We examined intercadherin interactions in epithelial A-431 cells producing endogenous E-cadherin and recombinant forms of E-cadherin tagged either by myc or by flag epitopes. Three distinct E-cadherin complexes were found. The first is a conventional E-cadherin–catenin complex consisting of one E-cadherin molecule linked either to β-catenin/{alpha}-catenin or to plakoglobin/{alpha}-catenin dimers. The second is a lateral E-cadherin complex incorporating two E-cadherin– catenin conventional complexes combined in parallel fashion via dimerization of the NH2-terminal extracellular domain of E-cadherin. The third complex is likely to contain two E-cadherin–catenin conventional complexes derived from two opposing cells and arranged in an antiparallel fashion. Formation of the antiparallel but not lateral complex strictly depends on extracellular calcium and E-cadherin binding to catenins. Double amino acid substitution Trp156Ala/Val157Gly within the extracellular NH2-terminal E-cadherin domain completely abolished both lateral and antiparallel inter–E-cadherin association. These data support an idea that the antiparallel complex has the adhesion function. Furthermore, they allow us to suggest that antiparallel complexes derive from lateral dimers and this complex process requires catenins and calcium ions.

Key Words: cadherins • catenins • p120 • intercellular adhesion • epithelial cells

Abbreviations used in this paper: aa, amino acid(s).

N. Chitaev wanted to dedicate this work in memory of his mother V. Chitaeva. We thank A. Averbackh, G. Goldberg, A. Eisen, R. Troyanovsky, and J. Klingelhöfer (all from Washington University, St. Louis, MO), and A. Ljubimov (Cedars-Sinai Medical Center, Los Angeles, CA) for valuable discussion and W.W. Franke for providing us with HaCat cells and anti-desmoglein antibody.

Address all correspondence to Sergey Troyanovsky, Division of Dermatology, Washington University Medical School, Campus Box 8123, 660 South Euclid Ave., St. Louis, MO 63110. Tel.: (314) 362-8154. Fax: (314) 362-8159. E-mail: sergeyt{at}im.wustl.edu


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