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Cryo-EM structures of the TMEM16A calcium-activated chloride channel

Author

Listed:
  • Shangyu Dang

    (University of California, San Francisco)

  • Shengjie Feng

    (University of California, San Francisco)

  • Jason Tien

    (University of California, San Francisco)

  • Christian J. Peters

    (University of California, San Francisco)

  • David Bulkley

    (University of California, San Francisco)

  • Marco Lolicato

    (Cardiovascular Research Institute, University of California, San Francisco)

  • Jianhua Zhao

    (University of California, San Francisco)

  • Kathrin Zuberbühler

    (University of California, San Francisco)

  • Wenlei Ye

    (University of California, San Francisco)

  • Lijun Qi

    (University of California, San Francisco)

  • Tingxu Chen

    (University of California, San Francisco)

  • Charles S. Craik

    (University of California, San Francisco)

  • Yuh Nung Jan

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

  • Daniel L. Minor

    (University of California, San Francisco
    Cardiovascular Research Institute, University of California, San Francisco
    University of California, San Francisco
    Lawrence Berkeley National Laboratory, Berkeley)

  • Yifan Cheng

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

  • Lily Yeh Jan

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

Abstract

Electron cryo-microscopy density maps of mouse TMEM16A reconstituted in nanodiscs or solubilized in detergent reveal two functional states of calcium-activated chloride channels.

Suggested Citation

  • Shangyu Dang & Shengjie Feng & Jason Tien & Christian J. Peters & David Bulkley & Marco Lolicato & Jianhua Zhao & Kathrin Zuberbühler & Wenlei Ye & Lijun Qi & Tingxu Chen & Charles S. Craik & Yuh Nung, 2017. "Cryo-EM structures of the TMEM16A calcium-activated chloride channel," Nature, Nature, vol. 552(7685), pages 426-429, December.
    • Handle: RePEc:nat:nature:v:552:y:2017:i:7685:d:10.1038_nature25024
    DOI: 10.1038/nature25024
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    Citations

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    Cited by:

    1. Eliza S. Nieweglowska & Axel F. Brilot & Melissa Méndez-Moran & Claire Kokontis & Minkyung Baek & Junrui Li & Yifan Cheng & David Baker & Joseph Bondy-Denomy & David A. Agard, 2023. "The ϕPA3 phage nucleus is enclosed by a self-assembling 2D crystalline lattice," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Yuanyue Shan & Mengmeng Zhang & Meiyu Chen & Xinyi Guo & Ying Li & Mingfeng Zhang & Duanqing Pei, 2024. "Activation mechanisms of dimeric mechanosensitive OSCA/TMEM63 channels," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    3. 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.
    4. Baobin Li & Christopher M. Hoel & Stephen G. Brohawn, 2021. "Structures of tweety homolog proteins TTYH2 and TTYH3 reveal a Ca2+-dependent switch from intra- to intermembrane dimerization," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
    5. Xiaoli Yang & Zhanyu Ding & Lisi Peng & Qiuyue Song & Deyu Zhang & Fang Cui & Chuanchao Xia & Keliang Li & Hua Yin & Shiyu Li & Zhaoshen Li & Haojie Huang, 2022. "Cryo-EM structures reveal the activation and substrate recognition mechanism of human enteropeptidase," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    6. Weijia Sun & Shuai Guo & Yuheng Li & JianWei Li & Caizhi Liu & Yafei Chen & Xuzhao Wang & Yingjun Tan & Hua Tian & Cheng Wang & Ruikai Du & Guohui Zhong & Sai Shi & Biao Ma & Chang Qu & Jingxuan Fu & , 2022. "Anoctamin 1 controls bone resorption by coupling Cl− channel activation with RANKL-RANK signaling transduction," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    7. Kaihua Zhang & Hao Wu & Nicholas Hoppe & Aashish Manglik & Yifan Cheng, 2022. "Fusion protein strategies for cryo-EM study of G protein-coupled receptors," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    8. Mingfeng Zhang & Yuanyue Shan & Charles D. Cox & Duanqing Pei, 2023. "A mechanical-coupling mechanism in OSCA/TMEM63 channel mechanosensitivity," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    9. Andy K. M. Lam & Sonja Rutz & Raimund Dutzler, 2022. "Inhibition mechanism of the chloride channel TMEM16A by the pore blocker 1PBC," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    10. Shengjie Feng & Cristina Puchades & Juyeon Ko & Hao Wu & Yifei Chen & Eric E. Figueroa & Shuo Gu & Tina W. Han & Brandon Ho & Tong Cheng & Junrui Li & Brian Shoichet & Yuh Nung Jan & Yifan Cheng & Lil, 2023. "Identification of a drug binding pocket in TMEM16F calcium-activated ion channel and lipid scramblase," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    11. Zhongjie Ye & Nicola Galvanetto & Leonardo Puppulin & Simone Pifferi & Holger Flechsig & Melanie Arndt & Cesar Adolfo Sánchez Triviño & Michael Palma & Shifeng Guo & Horst Vogel & Anna Menini & Clemen, 2024. "Structural heterogeneity of the ion and lipid channel TMEM16F," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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