Visualizing the interior architecture of focal adhesions with high-resolution traction maps.
Visualizing the interior architecture of focal adhesions with high-resolution traction maps.
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DOI：
10.1021/nl5047335
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发表时间：
2015-04-08
期刊：
影响因子：
10.8
通讯作者：
Dunn AR
中科院分区：
文献类型：
--
作者：
Morimatsu M;Mekhdjian AH;Chang AC;Tan SJ;Dunn AR
局灶黏附（FAs）是微米级的蛋白质组合，协调细胞黏附、迁移和机械转导。FAs内的许多蛋白质是如何组织成力传感和传输结构的，目前还不清楚。我们将荧光分子张力传感器与超分辨率光学显微镜相结合，在<100 nm的空间分辨率下观察FAs内的牵引力。我们发现αvβ3整合素选择性地定位于高强度区域。Paxillin通常不被认为在力传递中起直接作用，但它与力的空间相关性高于血管蛋白、talin或α-肌动蛋白，后者被认为是力传感器。这些观察结果表明αvβ3整合素和paxillin可能在机械转导中起重要作用。
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.
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