Cadherin exits the junction by switching its adhesive bond

Soonjin Hong, Regina B. Troyanovsky, Sergey M. Troyanovsky*

*Corresponding author for this work

Research output: Contribution to journalArticle

56 Scopus citations

Abstract

The plasticity of cell-cell adhesive structures is crucial to all normal and pathological morphogenetic processes. The molecular principles of this plasticity remain unknown. Here we study the roles of two dimerization interfaces, the so-called strand-swap and X dimer interfaces of E-cadherin, in the dynamic remodeling of adherens junctions using photoactivation, calcium switch, and coimmunoprecipitation assays. We show that the targeted inactivation of the X dimer interface blocks the turnover of catenin-uncoupled cadherin mutants in the junctions of A-431 cells. In contrast, the junctions formed by strand-swap dimer interface mutants exhibit high instability. Collectively, our data demonstrate that the strand-swap interaction is a principal cadherin adhesive bond that keeps cells in firm contact. However, to leave the adherens junction, cadherin reconfigures its adhesive bond from the strand swap to the X dimer type. Such a structural transition, controlled by intercellular traction forces or by lateral cadherin alignment, may be the key event regulating adherens junction dynamics.

Original languageEnglish (US)
Pages (from-to)1073-1083
Number of pages11
JournalJournal of Cell Biology
Volume192
Issue number6
DOIs
StatePublished - Mar 21 2011

ASJC Scopus subject areas

  • Cell Biology

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