抄録
Adherens junction (AJ), which directly links actin cytosketons in adjacent cells, transmits tension derived from acto-myosin activities. As a mechano-sensitive molecule at AJ, α-catenin senses and balances intercellular tension. α-Catenin changes its conformation under intercellular tension and opens auto-inhibited structure for vinculin, resulting in a local actin remodeling. However, it is unknown how firmly α-catenin and vinculin interact with each other, both of which are exerted on intercellular tension. Also, little is known about changes in conformation and vinculin affinity after α-catenin opens auto-inhibited structure. Here, we measured binding force between α-catenin and vinculin by using single-molecule force spectroscopy employing atomic force microscopy. Furthermore, we revealed changes in the conformation of α-catenin and vinculin affinity. As a result, we revealed that activated α-catenin can firmly bind to vinculin. Furthermore, AFM images showed the drastic conformational changes occurred in α-catenin after opening auto-inhibited structure, resulting in increase in vinculin affinity.
