Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions

J. Klingelhofer, R. B. Troyanovsky, O. Y. Laur, S. Troyanovsky*

*Corresponding author for this work

Research output: Contribution to journalArticle

27 Scopus citations

Abstract

Classic cadherins are transmembrane receptors involved in cell type-specific calcium-dependent intercellular adhesion. The specificity of adhesion is mediated by homophilic interactions between cadherins extending from opposing cell surfaces. In addition, classic cadherins can self-associate forming lateral dimers. Whereas it is widely excepted that lateral dimerization of cadherins is critical for adhesion, details of this process are not known. Yet, no evidence for physical association between different classic cadherins in cells expressing complex cadherin patterns has been reported. To study lateral and adhesive intercadherin interactions, we examined interactions between two classic cadherins, E- and P-cadherins, in epithelial A-431 cells co-producing both proteins. We showed that these cells exhibited heterocomplexes consisting of laterally assembled E- and P-cadherins. These complexes were formed by a mechanism involving Trp156 of E-cadherin. Removal of calcium ions from the culture medium triggered a novel Trp156-independent type of lateral E-cadherin-P-cadherin association. Notably, an antiparallel (adhesive) mode of interaction between these cadherins was negligible. The specificity of adhesive interaction was localized to the amino-terminal (EC1) domain of both cadherins. Thus, EC1 domain of classic cadherins exposes two determinants responsible for nonspecific lateral and cadherin type-specific adhesive dimerization.

Original languageEnglish (US)
Pages (from-to)2829-2836
Number of pages8
JournalJournal of Cell Science
Volume113
Issue number16
StatePublished - Jan 1 2000

Keywords

  • Cadherin
  • Catenin
  • Intercellular adhesion

ASJC Scopus subject areas

  • Cell Biology

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