School of Physiology, Pharmacology and Neuroscience, Faculty of Life Sciences, University of Bristol, Bristol, United Kingdom.
School of Biochemistry, Faculty of Life Sciences, University of Bristol, Bristol, United Kingdom.
J Cell Biol. 2020 Sep 7;219(9). doi: 10.1083/jcb.201911154.
Microtubules and filamentous (F-) actin engage in complex interactions to drive many cellular processes from subcellular organization to cell division and migration. This is thought to be largely controlled by proteins that interface between the two structurally distinct cytoskeletal components. Here, we use cryo-electron tomography to demonstrate that the microtubule lumen can be occupied by extended segments of F-actin in small molecule-induced, microtubule-based, cellular projections. We uncover an unexpected versatility in cytoskeletal form that may prompt a significant development of our current models of cellular architecture and offer a new experimental approach for the in situ study of microtubule structure and contents.
微管和丝状(F)肌动蛋白之间存在复杂的相互作用,从亚细胞组织到细胞分裂和迁移,驱动着许多细胞过程。这被认为主要是由两种结构上不同的细胞骨架成分之间的界面蛋白控制的。在这里,我们使用低温电子断层扫描技术证明,在小分子诱导的基于微管的细胞突起中,微管腔可以被延伸的 F-肌动蛋白段占据。我们揭示了细胞骨架形态的一种出人意料的多功能性,这可能会促使我们对细胞结构的现有模型进行重大发展,并为微管结构和内容的原位研究提供一种新的实验方法。