| First Author | Bianchini JM | Year | 2015 |
| Journal | J Cell Biol | Volume | 210 |
| Issue | 7 | Pages | 1065-74 |
| PubMed ID | 26416960 | Mgi Jnum | J:227654 |
| Mgi Id | MGI:5702367 | Doi | 10.1083/jcb.201411080 |
| Citation | Bianchini JM, et al. (2015) Reevaluating alphaE-catenin monomer and homodimer functions by characterizing E-cadherin/alphaE-catenin chimeras. J Cell Biol 210(7):1065-74 |
| abstractText | As part of the E-cadherin-beta-catenin-alphaE-catenin complex (CCC), mammalian alphaE-catenin binds F-actin weakly in the absence of force, whereas cytosolic alphaE-catenin forms a homodimer that interacts more strongly with F-actin. It has been concluded that cytosolic alphaE-catenin homodimer is not important for intercellular adhesion because E-cadherin/alphaE-catenin chimeras thought to mimic the CCC are sufficient to induce cell-cell adhesion. We show that, unlike alphaE-catenin in the CCC, these chimeras homodimerize, bind F-actin strongly, and inhibit the Arp2/3 complex, all of which are properties of the alphaE-catenin homodimer. To more accurately mimic the junctional CCC, we designed a constitutively monomeric chimera, and show that E-cadherin-dependent cell adhesion is weaker in cells expressing this chimera compared with cells in which alphaE-catenin homodimers are present. Our results demonstrate that E-cadherin/alphaE-catenin chimeras used previously do not mimic alphaE-catenin in the native CCC, and imply that both CCC-bound monomer and cytosolic homodimer alphaE-catenin are required for strong cell-cell adhesion. |
