?-Catenin-mediated cadherin clustering couples cadherin and actin dynamics.

ABSTRACT: The function of the actin-binding domain of ?-catenin, ?ABD, 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 ?ABD surface that interfere with ?ABD binding to actin and used them to probe the role of ?-catenin-actin interactions in adherens junctions. We found that the junctions directly bound to actin via ?ABD were more dynamic than the junctions bound to actin indirectly through vinculin and that recombinant ?ABD interacted with cortical actin but not with actin bundles. This interaction resulted in the formation of numerous short-lived cortex-bound ?ABD clusters. Our data suggest that ?ABD 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 ?ABD 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.

SUBMITTER: Chen CS 

PROVIDER: S-EPMC4539995 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature