Vogel Sven K, Petrasek Zdenek, Heinemann Fabian, Schwille Petra
Max Planck Institute of Biochemistry , Department of Cellular and Molecular Biophysics , Martinsried , Germany.
Elife. 2013 Jan 8;2:e00116. doi: 10.7554/eLife.00116.
Cell cortex remodeling during cell division is a result of myofilament-driven contractility of the cortical membrane-bound actin meshwork. Little is known about the interaction between individual myofilaments and membrane-bound actin filaments. Here we reconstituted a minimal actin cortex to directly visualize the action of individual myofilaments on membrane-bound actin filaments using TIRF microscopy. We show that synthetic myofilaments fragment and compact membrane-bound actin while processively moving along actin filaments. We propose a mechanism by which tension builds up between the ends of myofilaments, resulting in compressive stress exerted to single actin filaments, causing their buckling and breakage. Modeling of this mechanism revealed that sufficient force (∼20 pN) can be generated by single myofilaments to buckle and break actin filaments. This mechanism of filament fragmentation and compaction may contribute to actin turnover and cortex reorganization during cytokinesis.DOI:http://dx.doi.org/10.7554/eLife.00116.001.
细胞分裂过程中的细胞皮层重塑是由皮质膜结合肌动蛋白网络的肌丝驱动收缩性导致的。关于单个肌丝与膜结合肌动蛋白丝之间的相互作用,我们了解得很少。在这里,我们重构了一个最小化的肌动蛋白皮层,以使用全内反射荧光显微镜(TIRF显微镜)直接观察单个肌丝对膜结合肌动蛋白丝的作用。我们发现,合成肌丝在沿着肌动蛋白丝进行性移动的同时,会使膜结合肌动蛋白片段化并使其致密化。我们提出了一种机制,即肌丝两端之间会产生张力,从而对单个肌动蛋白丝施加压缩应力,导致其弯曲和断裂。对该机制的建模表明,单个肌丝可以产生足够的力(约20皮牛)使肌动蛋白丝弯曲和断裂。这种丝片段化和致密化的机制可能有助于胞质分裂过程中的肌动蛋白周转和皮层重组。DOI:http://dx.doi.org/10.7554/eLife.00116.001 。