Architecture of the mammalian mechanosensitive Piezol channel
Architecture of the mammalian mechanosensitive Piezol channel
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DOI：
10.1038/nature15247
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发表时间：
2015-11-05
期刊：
影响因子：
64.8
通讯作者：
Yang, Maojun
中科院分区：
文献类型：
--
作者：
Ge, Jingpeng;Li, Wanqiu;Yang, Maojun
Piezo蛋白是进化上保守且功能多样的机械敏感阳离子通道。然而，压电通道的整体结构结构和门控机制仍不清楚。在这里，我们测定了全长(2,547个氨基酸)小鼠Piezol(Piezol)的冷冻电子显微镜结构，分辨率为4.8埃。Piezol形成一个三聚体螺旋桨状结构(约900kodalton)，胞外结构域类似于三个远端叶片和一个中心帽。跨膜区的每个亚基有14个明显可分辨的片段。这些部分形成三个外围翼和一个包围潜在离子传导孔的中央孔模块。相当灵活的细胞外叶片结构域通过三个长梁状结构连接到中央细胞内结构域。这种三聚体结构表明，Piezol可能会使用其外围区域作为力传感器来选通中央离子传导孔。
Piezo proteins are evolutionarily conserved and functionally diverse mechanosensitive cation channels. However, the overall structural architecture and gating mechanisms of Piezo channels have remained unknown. Here we determine the cryo-electron microscopy structure of the full-length (2,547 amino acids) mouse Piezol (Piezol) at a resolution of 4.8 angstrom. Piezol forms a trimeric propeller-like structure (about 900 kilodalton), with the extracellular domains resembling three distal blades and a central cap. The transmembrane region has 14 apparently resolved segments per subunit. These segments form three peripheral wings and a central pore module that encloses a potential ion-conducting pore. The rather flexible extracellular blade domains are connected to the central intracellular domain by three long beam-like structures. This trimeric architecture suggests that Piezol may use its peripheral regions as force sensors to gate the central ion-conducting pore.