IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v496y2013i7445d10.1038_nature12056.html
   My bibliography  Save this article

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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature12056
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature12056?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    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.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:496:y:2013:i:7445:d:10.1038_nature12056. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.