α-Catenin-mediated cadherin clustering couples cadherin and actin dynamics

Chi Shuo Chen, Soonjin Hong, Indrajyoti Indra, Alina P. Sergeeva, Regina B. Troyanovsky, Lawrence Shapiro, Barry Honig, Sergey M. Troyanovsky*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

The function of the actin-binding domain of α-catenin, αABD, including its possible role in the direct anchorage of the cadherin-catenin complex to the actin cytoskeleton, has remained uncertain. We identified two point mutations on the αABD surface that interfere with αABD binding to actin and used them to probe the role of α-catenin-actin interactions in adherens junctions. We found that the junctions directly bound to actin via αABD were more dynamic than the junctions bound to actin indirectly through vinculin and that recombinant αABD interacted with cortical actin but not with actin bundles. This interaction resulted in the formation of numerous short-lived cortex-bound αABD clusters. Our data suggest that αABD clustering drives the continuous assembly of transient, actin-associated cadherin-catenin clusters whose disassembly is maintained by actin depolymerization. It appears then that such actin-dependent αABD clustering is a unique molecular mechanism mediating both integrity and reassembly of the cell-cell adhesive interface formed through weak cis- and trans-intercadherin interactions.

Original languageEnglish (US)
Pages (from-to)647-661
Number of pages15
JournalJournal of Cell Biology
Volume210
Issue number4
DOIs
StatePublished - 2015

ASJC Scopus subject areas

  • Cell Biology

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