Abstract
Intercellular tension generated by actomyosin activities is transmitted between cells and induces reciprocal mechanotransduction, resulting to many biological processes such as morphogenesis, maintenance of tissue integrity and wound healing in which dynamic cell rearrangement and tissue deformation are undergone. Adherens junctions (AJs) and its component molecules are known to not only transmit the intercellular tension but also directly contribute to the intercellular mechanotransduction. According to previous researches, a-catenin would function as a mechanosensor at AJs, which mechanically response to the intercellular tension inducing vinculin, though its mechanical behaviors still remain unclear. In this study, we analyzed the mechanical properties of a-catenin by AFM-based single molecule force spectroscopy (SMFS) and revealed that a-catenin has a high mechanical responsiveness, which dynamically changes its conformation through a specific unfolding pathway under tension.
