Study of motile mechanism of myosin VI using high-speed atomic force microscopy

肌凝蛋白6是肌凝蛋白超家族中唯一移动到肌动蛋白丝负端的肌凝蛋白。有趣的是，我们知道肌凝蛋白6走路的步幅比他们脚长的预期要大。但由于缺乏结构证据，其作用机制尚未阐明。在这里，我们使用高速原子力显微镜来直接观察它们工作时肌球蛋白6的结构动力学。随后，首次获得了结构证据，从而更好地理解了肌球蛋白6的功能机制。

Myosin 6 is the only myosin among myosin superfamily that moves to the minus end of actin filament. Interestingly, it is known that myosin 6 walks with larger stride than that expected from their foot length. However, their functional mechanism has not been elucidated yet, due to the lack of structural evidence. Here, we performed high-speed atomic force microscopy to directly observe their structural dynamics of myosin 6 at work. Then, the structural evidence was successively obtained for the first time, leading to better understanding the functional mechanism of myosin 6.