阿杰初遇雯的时候,一场大雨正经过这个城市,雨水打在蛋糕店的橱窗上,蜿蜒而下,阿杰望着蒙在窗上的雾水,用手指在上面胡乱地画着,店里的音乐是 Roy Orbison的PrettyWoman,阿杰冥想着一个女孩,水一样的长发,薄簿的嘴唇,嘴角上翘。阿杰在...阿杰初遇雯的时候,一场大雨正经过这个城市,雨水打在蛋糕店的橱窗上,蜿蜒而下,阿杰望着蒙在窗上的雾水,用手指在上面胡乱地画着,店里的音乐是 Roy Orbison的PrettyWoman,阿杰冥想着一个女孩,水一样的长发,薄簿的嘴唇,嘴角上翘。阿杰在空气中勾勒着,发现玻璃窗上真的浮现出这样的一张脸,阿杰抹去窗上的雾气,一身雨水的雯便清晰地出现在阿杰的视线里了。雯在阿杰的蛋糕店里点了一杯牛奶。展开更多
Talin is an integrin-binding protein located at focal adhesion site and serves as both an adapter and a force transmitter. Its integrin binding activity is regulated by the intramolecular autoinhibition interaction be...Talin is an integrin-binding protein located at focal adhesion site and serves as both an adapter and a force transmitter. Its integrin binding activity is regulated by the intramolecular autoinhibition interaction between its F3 and RS domains. Here, we used atomic force microscopy to measure the strength of talin autoinhibition complex. Our results suggest that the lifetime of talin autoinhibition complex shows weak catch bond behavior and does not change significantly at smaller forces, while it drops rapidly at larger forces(>10 p N). Moreover, besides the complex conformation revealed by crystal structure, our molecular dynamics(MD) simulations indicate the possible existence of another stable conformation. Further analysis indicates that forces may regulate the equilibrium of the two stable binding states and result in the non-exponential force dependence of the binding lifetime. Our findings reveal a negative regulation mechanism on talin activation and provide a new point of view on the function of talin in focal adhesion.展开更多
文摘阿杰初遇雯的时候,一场大雨正经过这个城市,雨水打在蛋糕店的橱窗上,蜿蜒而下,阿杰望着蒙在窗上的雾水,用手指在上面胡乱地画着,店里的音乐是 Roy Orbison的PrettyWoman,阿杰冥想着一个女孩,水一样的长发,薄簿的嘴唇,嘴角上翘。阿杰在空气中勾勒着,发现玻璃窗上真的浮现出这样的一张脸,阿杰抹去窗上的雾气,一身雨水的雯便清晰地出现在阿杰的视线里了。雯在阿杰的蛋糕店里点了一杯牛奶。
基金supported by the National Basic Research Program of China(2014CB910202)National Natural Science Foundation of China(11302240,31070827 and 31222022)
文摘Talin is an integrin-binding protein located at focal adhesion site and serves as both an adapter and a force transmitter. Its integrin binding activity is regulated by the intramolecular autoinhibition interaction between its F3 and RS domains. Here, we used atomic force microscopy to measure the strength of talin autoinhibition complex. Our results suggest that the lifetime of talin autoinhibition complex shows weak catch bond behavior and does not change significantly at smaller forces, while it drops rapidly at larger forces(>10 p N). Moreover, besides the complex conformation revealed by crystal structure, our molecular dynamics(MD) simulations indicate the possible existence of another stable conformation. Further analysis indicates that forces may regulate the equilibrium of the two stable binding states and result in the non-exponential force dependence of the binding lifetime. Our findings reveal a negative regulation mechanism on talin activation and provide a new point of view on the function of talin in focal adhesion.
