Actin cytoskeleton contractility plays a critical role in morphogenetic processes by generating forces that are then transmitted to cell–cell and cell-ECM adhesion complexes. In turn, mechanical properties of the environment are sensed and transmitted to the cytoskeleton at cell adhesion sites, influencing cellular processes such as cell migration, differentiation and survival. Anchoring of the actomyosin cytoskeleton to adhesion sites is mediated by adaptor proteins such as talin or α-catenin that link F-actin to transmembrane cell adhesion receptors, thereby allowing mechanical coupling between the intracellular and extracellular compartments. Thus, a key issue is to be able to measure the forces generated by actomyosin and transmitted to the adhesion complexes. Approaches developed in cells and those probing single molecule mechanical properties of α-catenin molecules allowed to identify α-catenin, an F-actin binding protein which binds to the cadherin complexes as a major player in cadherin-based mechanotransduction. However, it is still very difficult to bridge intercellular forces measured at cellular levels and those measured at the single-molecule level.

中文翻译：

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直接测量由结合 α-连环蛋白的自组织肌动球蛋白纤维产生的近纳米牛顿力

肌动蛋白细胞骨架收缩性通过产生力在形态发生过程中发挥关键作用，然后将力传递到细胞-细胞和细胞-ECM 粘附复合物。反过来，环境的机械特性被感知并传递到细胞粘附位点的细胞骨架，影响细胞迁移、分化和存活等细胞过程。肌动球蛋白细胞骨架与粘附位点的锚定是由衔接蛋白（如 talin 或 α-连环蛋白）介导的，它们将 F-肌动蛋白与跨膜细胞粘附受体连接起来，从而允许细胞内和细胞外区室之间的机械耦合。因此，一个关键问题是能够测量由肌动球蛋白产生并传递到粘附复合物的力。在细胞中开发的方法和探索 α-连环蛋白分子的单分子机械特性的方法允许识别 α-连环蛋白，一种与钙粘蛋白复合物结合的 F-肌动蛋白结合蛋白，是基于钙粘蛋白的机械转导的主要参与者。然而，在细胞水平上测量的细胞间力和在单分子水平上测量的细胞间力仍然非常困难。