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Electron cryo-microscopy structure of the mechanotransduction channel NOMPC

Author

Listed:
  • Peng Jin

    (University of California)

  • David Bulkley

    (University of California)

  • Yanmeng Guo

    (University of California)

  • Wei Zhang

    (University of California
    Howard Hughes Medical Institute, University of California)

  • Zhenhao Guo

    (University of California)

  • Walter Huynh

    (University of California)

  • Shenping Wu

    (Howard Hughes Medical Institute, University of California)

  • Shan Meltzer

    (University of California)

  • Tong Cheng

    (University of California
    Howard Hughes Medical Institute, University of California)

  • Lily Yeh Jan

    (University of California
    University of California
    Howard Hughes Medical Institute, University of California)

  • Yuh-Nung Jan

    (University of California
    University of California
    Howard Hughes Medical Institute, University of California)

  • Yifan Cheng

    (University of California
    Howard Hughes Medical Institute, University of California)

Abstract

Single-particle electron cryo-microscopy analysis of the mechanotransduction channel NOMPC reveals that it contains a bundle of four helical spring-shaped ankyrin repeat domains that undergo motion, potentially allowing mechanical movement of the cytoskeleton to be coupled to the opening of the channel.

Suggested Citation

  • Peng Jin & David Bulkley & Yanmeng Guo & Wei Zhang & Zhenhao Guo & Walter Huynh & Shenping Wu & Shan Meltzer & Tong Cheng & Lily Yeh Jan & Yuh-Nung Jan & Yifan Cheng, 2017. "Electron cryo-microscopy structure of the mechanotransduction channel NOMPC," Nature, Nature, vol. 547(7661), pages 118-122, July.
    • Handle: RePEc:nat:nature:v:547:y:2017:i:7661:d:10.1038_nature22981
    DOI: 10.1038/nature22981
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    Cited by:

    1. Yuqi Qin & Daqi Yu & Dan Wu & Jiangqing Dong & William Thomas Li & Chang Ye & Kai Chit Cheung & Yingyi Zhang & Yun Xu & YongQiang Wang & Yun Stone Shi & Shangyu Dang, 2023. "Cryo-EM structure of TMEM63C suggests it functions as a monomer," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    2. Zhengyang Kong & Elvis K. Boahen & Dong Jun Kim & Fenglong Li & Joo Sung Kim & Hyukmin Kweon & So Young Kim & Hanbin Choi & Jin Zhu & Wu Ying & Do Hwan Kim, 2024. "Ultrafast underwater self-healing piezo-ionic elastomer via dynamic hydrophobic-hydrolytic domains," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    3. Martina Nicoletti & Letizia Chiodo & Alessandro Loppini, 2021. "Biophysics and Modeling of Mechanotransduction in Neurons: A Review," Mathematics, MDPI, vol. 9(4), pages 1-32, February.

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