IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v11y2020i1d10.1038_s41467-020-16842-0.html
   My bibliography  Save this article

A constricted opening in Kir channels does not impede potassium conduction

Author

Listed:
  • Katrina A. Black

    (The Walter and Eliza Hall Institute of Medical Research
    The University of Melbourne)

  • Sitong He

    (La Trobe University)

  • Ruitao Jin

    (La Trobe University)

  • David M. Miller

    (The Walter and Eliza Hall Institute of Medical Research
    The University of Melbourne)

  • Jani R. Bolla

    (University of Oxford)

  • Oliver B. Clarke

    (Columbia University)

  • Paul Johnson

    (The University of Newcastle)

  • Monique Windley

    (Victor Chang Cardiac Research Institute)

  • Christopher J. Burns

    (The University of Melbourne
    The Walter and Eliza Hall Institute of Medical Research)

  • Adam P. Hill

    (Victor Chang Cardiac Research Institute)

  • Derek Laver

    (The University of Newcastle)

  • Carol V. Robinson

    (University of Oxford)

  • Brian J. Smith

    (La Trobe University)

  • Jacqueline M. Gulbis

    (The Walter and Eliza Hall Institute of Medical Research
    The University of Melbourne)

Abstract

The canonical mechanistic model explaining potassium channel gating is of a conformational change that alternately dilates and constricts a collar-like intracellular entrance to the pore. It is based on the premise that K+ ions maintain a complete hydration shell while passing between the transmembrane cavity and cytosol, which must be accommodated. To put the canonical model to the test, we locked the conformation of a Kir K+ channel to prevent widening of the narrow collar. Unexpectedly, conduction was unimpaired in the locked channels. In parallel, we employed all-atom molecular dynamics to simulate K+ ions moving along the conduction pathway between the lower cavity and cytosol. During simulations, the constriction did not significantly widen. Instead, transient loss of some water molecules facilitated K+ permeation through the collar. The low free energy barrier to partial dehydration in the absence of conformational change indicates Kir channels are not gated by the canonical mechanism.

Suggested Citation

  • Katrina A. Black & Sitong He & Ruitao Jin & David M. Miller & Jani R. Bolla & Oliver B. Clarke & Paul Johnson & Monique Windley & Christopher J. Burns & Adam P. Hill & Derek Laver & Carol V. Robinson , 2020. "A constricted opening in Kir channels does not impede potassium conduction," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16842-0
    DOI: 10.1038/s41467-020-16842-0
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-020-16842-0
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-020-16842-0?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. Johansen B. Amin & Miaomiao He & Ramesh Prasad & Xiaoling Leng & Huan-Xiang Zhou & Lonnie P. Wollmuth, 2023. "Two gates mediate NMDA receptor activity and are under subunit-specific regulation," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    2. Félix-Martínez, G.J. & Picones, A. & Godínez-Fernández, J.R., 2024. "Short and long-range correlations in single-channel currents from inwardly rectifying K+ channels," Chaos, Solitons & Fractals, Elsevier, vol. 178(C).

    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_s41467-020-16842-0. 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.