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Visualizing the interior architecture of focal adhesions with high-resolution traction maps

机译:用高分辨率牵引图可视化粘着的内部结构

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摘要

Focal adhesions (FAs) are micron-sized protein assemblies that coordinate cell adhesion, migration, and mechanotransduction. How the many proteins within FAs are organized into force sensing and transmitting structures is poorly understood. We combined fluorescent molecular tension sensors with super-resolution light microscopy to visualize traction forces within FAs with <100 nm spatial resolution. We find that αvβ3 integrin selectively localizes to high force regions. Paxillin, which is not generally considered to play a direct role in force transmission, shows a higher degree of spatial correlation with force than vinculin, talin, or α-actinin, proteins with hypothesized roles as force transducers. These observations suggest that αvβ3 integrin and paxillin may play important roles in mechanotransduction.
机译:局灶性粘附(FAs)是微米大小的蛋白质装配体,可协调细胞粘附,迁移和机械转导。人们对FA中许多蛋白质如何组织成力感测和传递结构的了解很少。我们将荧光分子张力传感器与超高分辨率光学显微镜相结合,以可视化方式在FA中以小于100 nm的空间分辨率观察牵引力。我们发现αvβ3整联蛋白选择性地定位于高强度区域。通常不认为Paxillin在力传递中起直接作用,但与具有假设的力传感器作用的新蛋白,talin或α-actinin蛋白相比,与力的空间相关性更高。这些观察结果表明αvβ3整联蛋白和paxillin可能在机械转导中起重要作用。

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