Craig D. Buckley, Jiongyi Tan, Karen L. Anderson, Dorit Hanein, Niels Volkmann, William I. Weis, W. James Nelson, Alexander R. Dunn
Cadherins are an ancient class of transmembrane proteins that are essential for the formation of multicellular tissues in metazoans. Cadherins link intercellular adhesions to the cellular cytoskeleton, but how they are connected specifically to actin filaments is a hotly debated issue. Genetic and cell culture experiments indicate that E-cadherin, β-catenin, and the actin filament binding protein αE-catenin form a minimal cadherin-catenin complex that binds to the actin cytoskeleton directly in epithelial tissues. However, experiments with purified proteins showed that a stable cadherin-catenin complex can be reconstituted, but it does not bind strongly to actin filaments in solution. Nevertheless, cell culture experiments indicated that the cadherin-catenin complex is under constitutive actomyosin-generated tension and that this connection is required for mechanotransduction at cadherin-based adhesions. Here, we tested the hypothesis that tension is required to stabilize a linkage between the cadherin-catenin complex and actin filaments, and clarify how the cadherin-catenin complex could interact directly with the actin cytoskeleton in cells.
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