The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex.
The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex.
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DOI：
10.1083/jcb.201304052
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发表时间：
2013-07-22
期刊：
影响因子：
--
通讯作者：
Carreno S
中科院分区：
文献类型：
--
作者：
Solinet S;Mahmud K;Stewman SF;Ben El Kadhi K;Decelle B;Talje L;Ma A;Kwok BH;Carreno S
ERM蛋白Moesin与微管的直接相互作用是中期纺锤体组织和后期细胞形态转化所必需的。Ezrin、Radixin和Moesin(ERM)蛋白在包括细胞分裂在内的许多细胞过程中发挥着重要作用。最近的研究强调了它们在癌症中的转移潜力。ERM在这些过程中的作用很大程度上归因于它们将肌动蛋白细丝连接到质膜的能力。在本文中，我们证明了ERM蛋白Moesin在体外直接与微管结合，并在体内稳定细胞皮质的微管。我们在ERM的FERM(4.1蛋白和ERM)结构域中发现了两个进化上保守的残基，它们介导了与微管的联系。这种ERM-微管相互作用是调节中期纺锤体组织和后期细胞形态转变所必需的，但对于连接肌动蛋白细丝到中期皮质是必不可少的。这些发现为理解有丝分裂中ERM蛋白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，并在需要ERM的生理和病理过程中具有广泛的意义。
The direct interaction between the ERM protein Moesin and microtubules is required for spindle organization in metaphase and cell shape transformation after anaphase onset. 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.
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