Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10.

Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10.
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DOI:
10.1038/s41467-023-42117-5
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发表时间:
2023-10-07
影响因子:
16.6
通讯作者:
Yuan, Peng
Yuan, Peng
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Zhang, Jingying;Maksaev, Grigory;Yuan, Peng

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植物在生长和发育过程中受到截然不同的渗透环境的挑战。对这些环境的适应通常涉及可以检测和响应机械力的机械敏感离子通道。在模式植物拟南芥中,机械敏感通道MSL10在低渗休克适应和程序性细胞死亡诱导中起着至关重要的作用,但通道功能的分子基础仍然知之甚少。在这里,我们报告了MSL10的结构和电生理分析。冷冻电子显微镜结构揭示了一个独特的七聚体通道组件。在洗涤剂和脂质环境中的野生型通道的结构,并在膜张力的情况下,捕获开放构象。此外,非导电突变体通道的结构分析表明,苯丙氨酸侧链单独的重新取向,没有主链重排,可能会产生疏水门。总之,这些结果揭示了一个独特的门控机制,并推进了我们对机械转导的理解。拟南芥机械敏感通道MSL10在低渗休克适应和程序性细胞死亡诱导中起着至关重要的作用。在这里,作者揭示了MSL10通道门控的结构机制。
Plants are challenged by drastically different osmotic environments during growth and development. Adaptation to these environments often involves mechanosensitive ion channels that can detect and respond to mechanical force. In the model plant Arabidopsis thaliana, the mechanosensitive channel MSL10 plays a crucial role in hypo-osmotic shock adaptation and programmed cell death induction, but the molecular basis of channel function remains poorly understood. Here, we report a structural and electrophysiological analysis of MSL10. The cryo-electron microscopy structures reveal a distinct heptameric channel assembly. Structures of the wild-type channel in detergent and lipid environments, and in the absence of membrane tension, capture an open conformation. Furthermore, structural analysis of a non-conductive mutant channel demonstrates that reorientation of phenylalanine side chains alone, without main chain rearrangements, may generate the hydrophobic gate. Together, these results reveal a distinct gating mechanism and advance our understanding of mechanotransduction. The Arabidopsis mechanosensitive channel MSL10 plays a crucial role in hypo-osmotic shock adaptation and programmed cell death induction. Here, the authors reveal the structural mechanism underlying MSL10 channel gating.
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