| First Author | Desai R | Year | 2013 |
| Journal | Nat Cell Biol | Volume | 15 |
| Issue | 3 | Pages | 261-73 |
| PubMed ID | 23417122 | Mgi Jnum | J:195204 |
| Mgi Id | MGI:5476862 | Doi | 10.1038/ncb2685 |
| Citation | Desai R, et al. (2013) Monomeric alpha-catenin links cadherin to the actin cytoskeleton. Nat Cell Biol 15(3):261-73 |
| abstractText | The linkage of adherens junctions to the actin cytoskeleton is essential for cell adhesion. The contribution of the cadherin-catenin complex to the interaction between actin and the adherens junction remains an intensely investigated subject that centres on the function of alpha-catenin, which binds to cadherin through beta-catenin and can bind F-actin directly or indirectly. Here, we delineate regions within Drosophila alpha-Catenin (alpha-Cat) that are important for adherens junction performance in static epithelia and dynamic morphogenetic processes. Moreover, we address whether persistent alpha-catenin-mediated physical linkage between cadherin and F-actin is crucial for cell adhesion and characterize the functions of alpha-catenin monomers and dimers at adherens junctions. Our data support the view that monomeric alpha-catenin acts as an essential physical linker between the cadherin-beta-catenin complex and the actin cytoskeleton, whereas alpha-catenin dimers are cytoplasmic and form an equilibrium with monomeric junctional alpha-catenin. |
