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Gating of the TrkH ion channel by its associated RCK protein TrkA

Author

Listed:
  • Yu Cao

    (College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, New York 10032, USA)

  • Yaping Pan

    (College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, New York 10032, USA
    Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA)

  • Hua Huang

    (College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, New York 10032, USA
    Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA)

  • Xiangshu Jin

    (National Institute of Biological Sciences)

  • Elena J. Levin

    (College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, New York 10032, USA
    Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA)

  • Brian Kloss

    (New York Consortium on Membrane Protein Structure, New York Structural Biology Center)

  • Ming Zhou

    (College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, New York 10032, USA
    Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA)

Abstract

TrkH belongs to a superfamily of K+ transport proteins required for growth of bacteria in low external K+ concentrations. The crystal structure of TrkH from Vibrio parahaemolyticus showed that TrkH resembles a K+ channel and may have a gating mechanism substantially different from K+ channels. TrkH assembles with TrkA, a cytosolic protein comprising two RCK (regulate the conductance of K+) domains, which are found in certain K+ channels and control their gating. However, fundamental questions on whether TrkH is an ion channel and how it is regulated by TrkA remain unresolved. Here we show single-channel activity of TrkH that is upregulated by ATP via TrkA. We report two structures of the tetrameric TrkA ring, one in complex with TrkH and one in isolation, in which the ring assumes two markedly different conformations. These results suggest a mechanism for how ATP increases TrkH activity by inducing conformational changes in TrkA.

Suggested Citation

  • Yu Cao & Yaping Pan & Hua Huang & Xiangshu Jin & Elena J. Levin & Brian Kloss & Ming Zhou, 2013. "Gating of the TrkH ion channel by its associated RCK protein TrkA," Nature, Nature, vol. 496(7445), pages 317-322, April.
    • Handle: RePEc:nat:nature:v:496:y:2013:i:7445:d:10.1038_nature12056
    DOI: 10.1038/nature12056
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    Cited by:

    1. Michał Uflewski & Tobias Rindfleisch & Kübra Korkmaz & Enrico Tietz & Sarah Mielke & Viviana Correa Galvis & Beatrix Dünschede & Marcin Luzarowski & Aleksandra Skirycz & Markus Schwarzländer & Deserah, 2024. "The thylakoid proton antiporter KEA3 regulates photosynthesis in response to the chloroplast energy status," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Wesley Tien Chiang & Yao-Kai Chang & Wei-Han Hui & Shu-Wei Chang & Chen-Yi Liao & Yi-Chuan Chang & Chun-Jung Chen & Wei-Chen Wang & Chien-Chen Lai & Chun-Hsiung Wang & Siou-Ying Luo & Ya-Ping Huang & , 2024. "Structural basis and synergism of ATP and Na+ activation in bacterial K+ uptake system KtrAB," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    3. Ashutosh Gulati & Surabhi Kokane & Annemarie Perez-Boerema & Claudia Alleva & Pascal F. Meier & Rei Matsuoka & David Drew, 2024. "Structure and mechanism of the K+/H+ exchanger KefC," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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