Cellular Mechanisms of Morphogenesis during Mitosis and Cell Motility, Université de Montréal, Montréal, Québec H3C 3J7, Canada.
J Cell Biol. 2013 Jul 22;202(2):251-60. doi: 10.1083/jcb.201304052. Epub 2013 Jul 15.
Ezrin, Radixin, and Moesin (ERM) proteins play important roles in many cellular processes including cell division. Recent studies have highlighted the implications of their metastatic potential in cancers. ERM's role in these processes is largely attributed to their ability to link actin filaments to the plasma membrane. In this paper, we show that the ERM protein Moesin directly binds to microtubules in vitro and stabilizes microtubules at the cell cortex in vivo. We identified two evolutionarily conserved residues in the FERM (4.1 protein and ERM) domains of ERMs that mediated the association with microtubules. This ERM-microtubule interaction was required for regulating spindle organization in metaphase and cell shape transformation after anaphase onset but was dispensable for bridging actin filaments to the metaphase cortex. These findings provide a molecular framework for understanding the complex functional interplay between the microtubule and actin cytoskeletons mediated by ERM proteins in mitosis and have broad implications in both physiological and pathological processes that require ERMs.
埃兹蛋白、radixin 和膜突蛋白（ERM）在许多细胞过程中发挥重要作用，包括细胞分裂。最近的研究强调了它们在癌症中的转移潜能的意义。ERM 在这些过程中的作用主要归因于它们将肌动蛋白丝连接到质膜的能力。在本文中，我们表明 ERM 蛋白膜突蛋白在体外直接结合微管，并在体内稳定细胞皮层处的微管。我们鉴定了 ERM 的 FERM（4.1 蛋白和 ERM）结构域中的两个进化保守残基，介导了与微管的结合。这种 ERM-微管相互作用对于调节中期纺锤体的组织以及后期起始后的细胞形状转化是必需的，但对于将肌动蛋白丝桥接到中期皮质是可有可无的。这些发现为理解 ERM 蛋白在有丝分裂中介导的微管和肌动蛋白细胞骨架之间复杂的功能相互作用提供了一个分子框架，并对需要 ERM 的生理和病理过程具有广泛的意义。
