Morimatsu Masatoshi, Mekhdjian Armen H, Chang Alice C, Tan Steven J, Dunn Alexander R
†Department of Chemical Engineering, Stanford University, Stanford, California 94305, United States.
‡Stanford Cardiovascular Institute, Stanford University School of Medicine, Stanford, California 94305, United States.
Nano Lett. 2015 Apr 8;15(4):2220-8. doi: 10.1021/nl5047335. Epub 2015 Mar 23.
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.
粘着斑（FAs）是微米级的蛋白质聚集体，可协调细胞粘附、迁移和机械转导。粘着斑内众多蛋白质如何组织成力传感和传递结构，目前尚不清楚。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，以<100 nm的空间分辨率可视化粘着斑内的牵引力。我们发现αvβ3整合素选择性定位于高力区域。桩蛋白通常不被认为在力传递中起直接作用，但与假定为力转导器的纽蛋白、踝蛋白或α-辅肌动蛋白相比，它与力的空间相关性更高。这些观察结果表明，αvβ3整合素和桩蛋白可能在机械转导中发挥重要作用。
