Editorial Overview: Myosins in Review.
Editorial Overview: Myosins in Review.
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编辑概述：肌球蛋白回顾。
DOI：
10.1111/tra.12405
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发表时间：
2016
期刊：
影响因子：
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通讯作者：
Kendrick-Jones J
中科院分区：
文献类型：
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作者：
Kendrick-Jones J
肌凝蛋白超家族由30多种基于肌动蛋白的运动蛋白组成，这些运动蛋白在广泛的复杂细胞过程中发挥作用，例如肌肉收缩、细胞运动、膜运输、细胞质分裂、细胞骨架结构和张力维持等（1,2）。为了完成这些细胞任务，人类已经进化出表达12类39种肌球蛋白(3)。为了确定不同类型的非常规（非肌肉）肌凝蛋白在几乎所有细胞通路中的特定分子作用，有必要了解这些马达如何适应其运动特性，它们如何选择特定的货物，以及它们的活动如何通过货物附着或通过它们的肌动蛋白丝轨迹进行调节。因此，这组综述捕获并总结了关于运动-货物复合物形成、运动活动调节和运动周期变化的重要新见解，所有这些都允许不同类别的肌凝蛋白执行不同的功能，例如自噬途径。李及其同事（李建超，卢清，张明杰）首次综述。细胞运输中非常规肌球蛋白对货物识别的结构基础。交通2016:DOI: 10.1111/tra。12383)总结了I、V、VI和X类肌凝蛋白单独或与特定货物结合时尾部结构域的最新高分辨率结构数据（4,5）。这些结构说明了非常规肌凝蛋白识别其货物的不同机制。作者提出了货物结合如何调节这些肌球蛋白在细胞运输途径中的活性的模型。然而，到目前为止，关于确定不同肌球蛋白如何调节货物结合和释放以确保初始摄取然后在准确的时间递送到细胞中正确位置的实际机制知之甚少。最近在高分辨率冷冻电镜成像、单分子生物物理方法和改进的结构分析技术以及细胞生物学分析方面的改进应该为这些重要问题提供有用的线索。Batters和Veigel的综述（Christopher Batters和Claudia Veigel， Mechanics and activation of unconventional myosins, Traffic 2016; DOI: 10.1111/tra）。12400)讨论了不同的结构区域（运动域，杠杆臂和尾部）的作用
The myosin superfamily is composed of more than 30 classes of actin-based motor proteins that play a role in a wide spectrum of complex cellular processes, such as muscle contraction, cell locomotion, membrane trafficking, cytokinesis, cytoskeletal structure and tension maintenance to name just a few (1, 2). To accomplish these cellular tasks, humans have evolved to express 39 myosins belonging to 12 classes (3). To establish the specific molecular roles of the different classes of unconventional (non-muscle) myosins in nearly all cellular pathways, it is essential to understand how these motors have adapted their kinetic motor properties, how they select specific cargoes and how their activities are regulated by cargo attachment or through their actin filament tracks. This set of reviews therefore captures and summarises important new insights into the formation of motor-cargo complexes, regulation of motor activity and variations in the kinetic cycle, all of which allow the different classes of myosins to perform distinct functions such as in the autophagy pathway. The first review by Li and colleagues (Jianchao Li, Qing Lu and Mingjie Zhang. Structural Basis of Cargo Recognition by Unconventional Myosins in Cellular Trafficking. Traffic 2016: DOI: 10.1111/tra. 12383) summarizes the most recent high-resolution structural data on the tail domains of myosins of class I, V, VI and X alone or when bound to specific cargo (4, 5). These structures illustrate the different mechanisms by which the unconventional myosins recognise their cargo. The authors present models of how cargo binding may regulate the activity of these myosins in cellular trafficking pathways. However, so far little is known about the actual mechanisms that determine how cargo binding and release is regulated by the different myosins to ensure initial uptake and then delivery at the exact time to the correct locations in the cell. Recent improvements in high-resolution cryo-EM imaging, single molecule biophysical methods and improved structural analysis techniques together with cell biological assays should provide useful clues to these important questions. The review by Batters and Veigel (Christopher Batters and Claudia Veigel, Mechanics and activation of unconventional myosins, Traffic 2016; DOI: 10.1111/tra. 12400) discusses the roles of the different structural regions (motor domain, lever arm and tail) on the