IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v11y2020i1d10.1038_s41467-020-14573-w.html
   My bibliography  Save this article

The Ca2+ permeation mechanism of the ryanodine receptor revealed by a multi-site ion model

Author

Listed:
  • Aihua Zhang

    (Peking University)

  • Hua Yu

    (Peking University)

  • Chunhong Liu

    (Peking University)

  • Chen Song

    (Peking University
    Peking University)

Abstract

Ryanodine receptors (RyR) are ion channels responsible for the release of Ca2+ from the sarco/endoplasmic reticulum and play a crucial role in the precise control of Ca2+ concentration in the cytosol. The detailed permeation mechanism of Ca2+ through RyR is still elusive. By using molecular dynamics simulations with a specially designed Ca2+ model, we show that multiple Ca2+ ions accumulate in the upper selectivity filter of RyR1, but only one Ca2+ can occupy and translocate in the narrow pore at a time, assisted by electrostatic repulsion from the Ca2+ within the upper selectivity filter. The Ca2+ is nearly fully hydrated with the first solvation shell intact during the whole permeation process. These results suggest a remote knock-on permeation mechanism and one-at-a-time occupation pattern for the hydrated Ca2+ within the narrow pore, uncovering the basis underlying the high permeability and low selectivity of the RyR channels.

Suggested Citation

  • Aihua Zhang & Hua Yu & Chunhong Liu & Chen Song, 2020. "The Ca2+ permeation mechanism of the ryanodine receptor revealed by a multi-site ion model," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14573-w
    DOI: 10.1038/s41467-020-14573-w
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-020-14573-w
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-020-14573-w?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
    ---><---

    Citations

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


    Cited by:

    1. B. U. Klink & A. Alavizargar & K. S. Kalyankumar & M. Chen & A. Heuer & C. Gatsogiannis, 2024. "Structural basis of α-latrotoxin transition to a cation-selective pore," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Simone Pelizzari & Martin C. Heiss & Monica L. Fernández-Quintero & Yousra El Ghaleb & Klaus R. Liedl & Petronel Tuluc & Marta Campiglio & Bernhard E. Flucher, 2024. "CaV1.1 voltage-sensing domain III exclusively controls skeletal muscle excitation-contraction coupling," Nature Communications, Nature, vol. 15(1), pages 1-13, 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:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14573-w. 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.