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A cryo-tomography-based volumetric model of the actin core of mouse vestibular hair cell stereocilia lacking plastin 1.
Journal of Structural Biology ( IF 3.0 ) Pub Date : 2020-01-18 , DOI: 10.1016/j.jsb.2020.107461 Junha Song 1 , Roma Patterson 1 , Zoltan Metlagel 1 , Jocelyn F Krey 2 , Samantha Hao 1 , Linshanshan Wang 1 , Brian Ng 1 , Salim Sazzed 3 , Julio Kovacs 4 , Willy Wriggers 4 , Jing He 3 , Peter G Barr-Gillespie 2 , Manfred Auer 1
Journal of Structural Biology ( IF 3.0 ) Pub Date : 2020-01-18 , DOI: 10.1016/j.jsb.2020.107461 Junha Song 1 , Roma Patterson 1 , Zoltan Metlagel 1 , Jocelyn F Krey 2 , Samantha Hao 1 , Linshanshan Wang 1 , Brian Ng 1 , Salim Sazzed 3 , Julio Kovacs 4 , Willy Wriggers 4 , Jing He 3 , Peter G Barr-Gillespie 2 , Manfred Auer 1
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Electron cryo-tomography allows for high-resolution imaging of stereocilia in their native state. Because their actin filaments have a higher degree of order, we imaged stereocilia from mice lacking the actin crosslinker plastin 1 (PLS1). We found that while stereocilia actin filaments run 13 nm apart in parallel for long distances, there were gaps of significant size that were stochastically distributed throughout the actin core. Actin crosslinkers were distributed through the stereocilium, but did not occupy all possible binding sites. At stereocilia tips, protein density extended beyond actin filaments, especially on the side of the tip where a tip link is expected to anchor. Along the shaft, repeating density was observed that corresponds to actin-to-membrane connectors. In the taper region, most actin filaments terminated near the plasma membrane. The remaining filaments twisted together to make a tighter bundle than was present in the shaft region; the spacing between them decreased from 13 nm to 9 nm, and the apparent filament diameter decreased from 6.4 to 4.8 nm. Our models illustrate detailed features of distinct structural domains that are present within the stereocilium.
中文翻译：
基于冷冻断层扫描的小鼠前庭毛细胞静纤毛肌动蛋白核心的体积模型，缺乏塑蛋白 1。
电子冷冻断层扫描可以对自然状态下的静纤毛进行高分辨率成像。由于肌动蛋白丝具有更高的有序度，我们对缺乏肌动蛋白交联剂塑蛋白 1 (PLS1) 的小鼠的静纤毛进行了成像。我们发现，虽然静纤毛肌动蛋白丝以 13 nm 的间隔平行运行很长的距离，但整个肌动蛋白核心中随机分布着相当大的间隙。肌动蛋白交联剂通过静纤毛分布，但并未占据所有可能的结合位点。在静纤毛尖端，蛋白质密度延伸到肌动蛋白丝之外，特别是在尖端链接预期锚定的尖端一侧。沿着轴，观察到对应于肌动蛋白到膜连接器的重复密度。在锥形区域，大多数肌动蛋白丝终止于质膜附近。剩余的细丝扭在一起形成比轴区域更紧的束；它们之间的间距从13 nm减小到9 nm，表观丝直径从6.4减小到4.8 nm。我们的模型展示了静纤毛中存在的不同结构域的详细特征。
更新日期：2020-03-26
中文翻译：
基于冷冻断层扫描的小鼠前庭毛细胞静纤毛肌动蛋白核心的体积模型，缺乏塑蛋白 1。
电子冷冻断层扫描可以对自然状态下的静纤毛进行高分辨率成像。由于肌动蛋白丝具有更高的有序度，我们对缺乏肌动蛋白交联剂塑蛋白 1 (PLS1) 的小鼠的静纤毛进行了成像。我们发现，虽然静纤毛肌动蛋白丝以 13 nm 的间隔平行运行很长的距离，但整个肌动蛋白核心中随机分布着相当大的间隙。肌动蛋白交联剂通过静纤毛分布，但并未占据所有可能的结合位点。在静纤毛尖端，蛋白质密度延伸到肌动蛋白丝之外，特别是在尖端链接预期锚定的尖端一侧。沿着轴，观察到对应于肌动蛋白到膜连接器的重复密度。在锥形区域，大多数肌动蛋白丝终止于质膜附近。剩余的细丝扭在一起形成比轴区域更紧的束；它们之间的间距从13 nm减小到9 nm，表观丝直径从6.4减小到4.8 nm。我们的模型展示了静纤毛中存在的不同结构域的详细特征。
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