One of the best known features of actin filaments is their helical structure. A number of essential properties emerge from this molecular arrangement of actin subunits. Here, we give an overview of the mechanical and biochemical implications of filament helicity, at different scales. In particular, a number of recent studies have highlighted the role of filament helicity in the adaptation to and the generation of mechanical torsion, and in the modulation of the filament's interaction with very different actin-binding proteins (such as myosins, cross-linkers, formins, and cofilin). Helicity can thus be seen as a key factor for the regulation of actin assembly, and as a link between biochemical regulators and their mechanical context. In addition, actin filament helicity appears to play an essential role in the establishment of chirality at larger scales, up to the organismal scale. Altogether, helicity appears to be an essential feature contributing to the regulation of actin assembly dynamics, and to actin's ability to organize cells at a larger scale.

中文翻译：

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肌动蛋白丝螺旋的许多含义。

肌动蛋白丝的最著名的特征之一是其螺旋结构。肌动蛋白亚基的这种分子排列产生了许多基本特性。在这里，我们给出了不同规模的丝螺旋性的机械和生化影响的概述。特别是，最近的许多研究都强调了丝线螺旋在适应和产生机械扭转以及在丝线与非常不同的肌动蛋白结合蛋白（例如肌球蛋白，交联剂，福明斯和cofilin）。因此，螺旋度可被视为调节肌动蛋白组装的关键因素，并且被视为生化调节剂与其机械环境之间的联系。此外，肌动蛋白丝的螺旋度似乎在建立更大的手性直至生物规模中都起着至关重要的作用。总而言之，螺旋性似乎是对肌动蛋白组装动力学的调节以及肌动蛋白大规模组织细胞的能力的重要特征。