Cadherin controls nectin recruitment into adherens junctions by remodeling the actin cytoskeleton

Regina B. Troyanovsky, Indrajyoti Indra, Chi Shuo Chen, Soonjin Hong, Sergey M. Troyanovsky*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


The mechanism that coordinates activities of different adhesion receptors is poorly understood. We investigated this mechanism by focusing on the nectin-2 and E-cadherin adherens junction receptors. We found that, cadherin was not required for the basic process of nectin junction formation because nectin-2 formed junctions in cadherin-deficient A431D cells. Formation of nectin-2 junctions in these cells, however, became regulated by cadherin as soon as E-cadherin was re-expressed. E-cadherin recruited nectin- 2 into adherens junctions, where both proteins formed distinct but tightly associated clusters. Live-cell imaging showed that the appearance of E-cadherin clusters often preceded that of nectin-2 clusters at sites of junction assembly. Inactivation of E-cadherin clustering by different strategies concomitantly suppressed the formation of nectin clusters. Furthermore, cadherin significantly increased the stability of nectin clusters, thereby making them resistant to the BC-12 antibody, which targets the nectin-2 adhesion interface. By testing different E-cadherin-α-catenin chimeras, we showed that the recruitment of nectin into chimera junctions is mediated by the actin-binding domain of α-catenin. Our data suggests that E-cadherin regulates assembly of nectin junctions through α-catenin-induced remodeling of the actin cytoskeleton around the cadherin clusters.

Original languageEnglish (US)
Pages (from-to)140-149
Number of pages10
JournalJournal of cell science
Issue number1
StatePublished - 2015


  • Actin
  • Adhesion
  • Cadherin
  • Nectin
  • α-catenin

ASJC Scopus subject areas

  • Cell Biology


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