Molecular basis of functional exchangeability between ezrin and other actin-membrane associated proteins during cytokinesis
Molecular basis of functional exchangeability between ezrin and other actin-membrane associated proteins during cytokinesis
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胞质分裂过程中埃兹蛋白和其他肌动蛋白膜相关蛋白之间功能交换的分子基础
DOI：
10.1016/j.yexcr.2021.112600
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发表时间：
2021
影响因子：
3.7
通讯作者：
Uehara Ryota
中科院分区：
文献类型：
--
作者：
Yang Guang;Hiruma Shota;Kitamura Akira;Kinjo Masataka;Mishra Mithilesh;Uehara Ryota
胞质分裂过程中介导收缩环和质膜之间相互作用的机制仍然难以捉摸。我们以前发现，ERM（Ezrin/Radixin/Moesin）蛋白，通常介导细胞极收缩，成为过度积累在细胞赤道和支持沟内陷后，其他肌动蛋白膜相关蛋白，苯胺和supervillin的损失。在这项研究中，我们解决了ezrin和其他肌动蛋白膜相关蛋白之间的交换介导的皮质收缩胞质分裂过程中的分子基础。我们发现，苯胺和supervillin的耗竭导致过度积累的膜相关的FERM结构域和肌动蛋白结合的C-末端结构域（C-端）的ezrin在卵裂沟，分别。这一发现表明，埃兹蛋白差异共享其结合位点与这些蛋白质的肌动蛋白细胞骨架或内膜表面。使用嵌合突变体，我们发现ezrin C-端，但不是FERM结构域，可以取代相应的苯胺结构域在胞质分裂和细胞增殖。另一方面，无论是膜相关的或肌动蛋白/肌球蛋白结合结构域的苯胺不能取代相应的埃兹蛋白结构域在控制皮质起泡在细胞两极。我们的研究结果突出了特定的设计肌动蛋白或膜相关的部分不同的肌动蛋白膜相关蛋白有限的交换，这使他们能够支持不同的皮质活动的共同肌动蛋白膜界面胞质分裂。
The mechanism that mediates the interaction between the contractile ring and the plasma membrane during cytokinesis remains elusive. We previously found that ERM (Ezrin/Radixin/Moesin) proteins, which usually mediate cellular pole contraction, become over-accumulated at the cell equator and support furrow ingression upon the loss of other actin-membrane associated proteins, anillin and supervillin. In this study, we addressed the molecular basis of the exchangeability between ezrin and other actin-membrane associated proteins in mediating cortical contraction during cytokinesis. We found that depletion of anillin and supervillin caused over-accumulation of the membrane-associated FERM domain and actin-binding C-terminal domain (C-term) of ezrin at the cleavage furrow, respectively. This finding suggests that ezrin differentially shares its binding sites with these proteins on the actin cytoskeleton or inner membrane surface. Using chimeric mutants, we found that ezrin C-term, but not the FERM domain, can substitute for the corresponding anillin domains in cytokinesis and cell proliferation. On the other hand, either the membrane-associated or the actin/myosin-binding domains of anillin could not substitute for the corresponding ezrin domains in controlling cortical blebbing at the cell poles. Our results highlight specific designs of actin- or membrane-associated moieties of different actin-membrane associated proteins with limited exchangeability, which enables them to support diverse cortical activities on the shared actin-membrane interface during cytokinesis.