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Originally published In Press as doi:10.1074/jbc.M101712200 on June 18, 2001

J. Biol. Chem., Vol. 276, Issue 33, 30862-30870, August 17, 2001
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Recognition of E-cadherin by Integrin alpha Ebeta 7
REQUIREMENT FOR CADHERIN DIMERIZATION AND IMPLICATIONS FOR CADHERIN AND INTEGRIN FUNCTION*

Elaine CorpsDagger , Christine CarterDagger , Paula KareclaDagger , Thomas Ahrens§, Paul EvansDagger , and Peter KilshawDagger

From the Dagger  Molecular Immunology Programme, The Babraham Institute, Babraham, Cambridge, CB2 4AT, United Kingdom and the § Department of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland

We have investigated the importance of dimerization of E-cadherin in the heterophilic adhesive interaction between E-cadherin and integrin alpha Ebeta 7. Dimerization of cadherin molecules in parallel alignment is known to be essential for homophilic adhesion and has been attributed to Ca2+-dependent interactions in the domain 1-2 junction or to cross-intercalation of Trp2 from one molecule to the other. We have disrupted either or both of these proposed mechanisms by point mutations in E-cadherin-Fc and have tested the modified proteins for alpha Ebeta 7-mediated cell adhesion. Prevention of Trp2 intercalation had no adverse effect on integrin-mediated adhesion, whereas disruption of Ca2+ binding permitted adhesion but with reduced efficiency. Both modifications in combination abolished recognition by alpha Ebeta 7. In EGTA, alpha Ebeta 7 adhered to wild type E-cadherin but not to the Trp2 deletion mutant. Independent evidence that the mutations prevented either or both mechanisms for dimerization is presented. The data show that dimerization is required for recognition by alpha Ebeta 7 and that it can take place by either of two mechanisms. Implications for the roles of the alpha E and beta 7 integrin subunits in ligand binding and for Trp2 and Ca2+ in the assembly of cadherin complexes are discussed.

* This work was supported by the Biotechnology and Biological Sciences Research Council, UK.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: The Babraham Institute, Babraham, Cambridge CB2 4AT, United Kingdom. Tel.: 44 1223 496553; Fax: 44 1223 496023; E-mail: peter.kilshaw@bbsrc.ac.uk.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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