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Electron cryo-microscopy structure of the mechanotransduction channel NOMPC

机译：机械转导通道NOMPC的电子低温显微镜结构

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摘要

Mechanosensory transduction for senses such as proprioception, touch, balance, acceleration, hearing and pain relies on mechanotransduction channels, which convert mechanical stimuli into electrical signals in specialized sensory cells(1). How force gates mechanotransduction channels is a central question in the field, for which there are two major models. One is the membrane-tension model: force applied to the membrane generates a change in membrane tension that is sufficient to gate the channel, as in the bacterial MscL channel and certain eukaryotic potassium channels(2-5). The other is the tether model: force is transmitted via a tether to gate the channel. The transient receptor potential (TRP) channel NOMPC is important for mechanosensation-related behaviours such as locomotion, touch and sound sensation across different species including Caenorhabditis elegans(6), Drosophila(7-9) and zebrafish(10). NOMPC is the founding member of the TRPN subfamily(11), and is thought to be gated by tethering of its ankyrin repeat domain to microtubules of the cytoskeleton(12-15). Thus, a goal of studying NOMPC is to reveal the underlying mechanism of force-induced gating, which could serve as a paradigm of the tether model. NOMPC fulfils all the criteria that apply to mechanotransduction channels(1,7) and has 29 ankyrin repeats, the largest number among TRP channels. A key question is how the long ankyrin repeat domain is organized as a tether that can trigger channel gating. Here we present a de novo atomic structure of Drosophila NOMPC determined by single-particle electron cryo-microscopy. Structural analysis suggests that the ankyrin repeat domain of NOMPC resembles a helical spring, suggesting its role of linking mechanical displacement of the cytoskeleton to the opening of the channel. The NOMPC architecture underscores the basis of translating mechanical force into an electrical signal within a cell.
机译：机械感觉转导用于本体感觉，触摸，平衡，加速度，听力和疼痛等感官，依赖于机械转导通道，该通道将机械刺激转换为专门的感觉细胞中的电信号（1）。力门机械传递通道的方式是该领域的中心问题，对此有两个主要模型。一种是膜张力模型：施加在膜上的力会产生足以控制通道的膜张力变化，例如细菌MscL通道和某些真核钾通道（2-5）。另一个是系绳模型：力通过系绳传递以控制通道。瞬态受体电位（TRP）通道NOMPC对于与机械感测相关的行为（例如秀丽隐杆线虫（6），果蝇（7-9）和斑马鱼（10））的运动，触觉和声音感觉至关重要。 NOMPC是TRPN家族的创始成员（11），被认为是通过将其锚蛋白重复结构域与细胞骨架的微管束缚来控制的（12-15）。因此，研究NOMPC的目标是揭示力门控的潜在机制，该机制可作为系链模型的范例。 NOMPC符合适用于机械转导通道的所有标准（1,7），并具有29个锚蛋白重复序列​​，在TRP通道中数量最多。一个关键问题是长锚蛋白重复域是如何组织成可触发通道门控的系链。在这里，我们介绍了通过单粒子电子冷冻显微镜测定的果蝇NOMPC的从头原子结构。结构分析表明，NOMPC的锚蛋白重复结构域类似于螺旋弹簧，表明其将细胞骨架的机械位移与通道的开放联系起来的作用。 NOMPC体系结构强调了将机械力转换为细胞内电信号的基础。

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  • 来源
    《Nature》 |2017年第7661期|118-122|共5页
  • 作者

    Jin Peng; Bulkley David; Guo Yanmeng; Zhang Wei; Guo Zhenhao; Huynh Walter; Wu Shenping; Meltzer Shan; Cheng Tong; Jan Lily Yeh; Jan Yuh-Nung; Cheng Yifan;

  • 作者单位

    Univ Calif San Francisco, Dept Physiol, San Francisco, CA 94158 USA;

    Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94158 USA;

    Univ Calif San Francisco, Dept Physiol, San Francisco, CA 94158 USA;

    Univ Calif San Francisco, Dept Physiol, San Francisco, CA 94158 USA|Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94158 USA;

    Univ Calif San Francisco, Dept Physiol, San Francisco, CA 94158 USA;

    Univ Calif San Francisco, Dept Cellular & Mol Pharmacol, San Francisco, CA 94158 USA;

    Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94158 USA;

    Univ Calif San Francisco, Dept Physiol, San Francisco, CA 94158 USA;

    Univ Calif San Francisco, Dept Physiol, San Francisco, CA 94158 USA|Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94158 USA;

    Univ Calif San Francisco, Dept Physiol, San Francisco, CA 94158 USA|Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94158 USA|Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94158 USA;

    Univ Calif San Francisco, Dept Physiol, San Francisco, CA 94158 USA|Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94158 USA|Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94158 USA;

    Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94158 USA|Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94158 USA;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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