Structural insights into microtubule doublet interactions in axonemes
Structural insights into microtubule doublet interactions in axonemes
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DOI：
10.1016/j.sbi.2007.03.013
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发表时间：
2007-04-01
影响因子：
6.8
通讯作者：
Sui, Haixin
中科院分区：
文献类型：
--
作者：
Downing, Kenneth H.;Sui, Haixin
动力蛋白马达驱动微管偶联体的协调滑动，产生真核生物纤毛和鞭毛的周期性跳动。最近的结构研究的轴丝，形成纤毛和鞭毛的核心，已经使用冷冻电子断层扫描，以揭示新的细节之间的相互作用的一些众多的蛋白质，形成轴丝和调节其运动。特别是几种动力蛋白之间的联系，表明它们的作用可能是协调的。孤立的双峰的分子结构的研究提供了一个结构基础，了解机械性能相关的轴丝的弯曲，也提供了深入了解的潜在作用的双峰动力蛋白活性调节的机制。
Coordinated sliding of microtubule doublets, driven by dynein motors, produces periodic beating of eukaryotic cilia and flagella. Recent structural studies of the axoneme, which forms the core of cilia and flagella, have used cryo-electron tomography to reveal new details of the interactions between some of the multitude of proteins that form the axoneme and regulate its movement. Connections between the several types of dyneins, in particular, suggest ways in which their action might be coordinated. Study of the molecular architecture of isolated doublets has provided a structural basis for understanding mechanical properties related to the bending of the axoneme, and has also offered insight into the potential role of doublets in the mechanism of dynein activity regulation.