IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v16y2025i1d10.1038_s41467-025-58443-9.html
   My bibliography  Save this article

Energy landscape of a Kv channel revealed by temperature steps while perturbing its electromechanical coupling

Author

Listed:
  • Bernardo I. Pinto-Anwandter

    (University of Chicago)

  • Carlos A. Z. Bassetto

    (University of Chicago
    The University of Texas at San Antonio)

  • Ramon Latorre

    (Universidad de Valparaiso)

  • Francisco Bezanilla

    (University of Chicago
    Universidad de Valparaiso)

Abstract

Voltage-dependent potassium channels (Kv) play a crucial role in membrane repolarization during action potentials. They undergo voltage-dependent structural conformational transitions according to their distribution across their energy landscape. Understanding these transitions helps us comprehend their molecular function. Here, we used sudden and sustained temperature changes (Tstep) combined with different voltage protocols and mutations to dissect the energy landscape of the Shaker K+ channel. We used two mutations, ILT (V369I, I372L, and S376T) and I384N, that affect the coupling between the voltage sensor (VSD) and the pore domain (PD), to obtain the temperature dependence of VSD last transition and the intrinsic temperature dependence of the pore, respectively. Our findings support a loose or tight conformation of the electromechanical coupling. In the loose conformation, the movement of the VSD is necessary but not sufficient to efficiently propagate the electromechanical energy to open the pore. In contrast, this movement is effectively translated into pore opening in the tight conformation. Our results describe the energy landscape of the Shaker channel and how its temperature dependence can be modulated by affecting its electromechanical coupling.

Suggested Citation

  • Bernardo I. Pinto-Anwandter & Carlos A. Z. Bassetto & Ramon Latorre & Francisco Bezanilla, 2025. "Energy landscape of a Kv channel revealed by temperature steps while perturbing its electromechanical coupling," Nature Communications, Nature, vol. 16(1), pages 1-14, December.
  • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-58443-9
    DOI: 10.1038/s41467-025-58443-9
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-025-58443-9
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-025-58443-9?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
    ---><---

    References listed on IDEAS

    as
    1. Zhe Lu & Angela M. Klem & Yajamana Ramu, 2001. "Ion conduction pore is conserved among potassium channels," Nature, Nature, vol. 413(6858), pages 809-813, October.
    2. João L. Carvalho-de-Souza & Francisco Bezanilla, 2019. "Noncanonical mechanism of voltage sensor coupling to pore revealed by tandem dimers of Shaker," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. repec:plo:pone00:0220415 is not listed on IDEAS
    2. Qiansheng Liang & Gamma Chi & Leonardo Cirqueira & Lianteng Zhi & Agostino Marasco & Nadia Pilati & Martin J. Gunthorpe & Giuseppe Alvaro & Charles H. Large & David B. Sauer & Werner Treptow & Manuel , 2024. "The binding and mechanism of a positive allosteric modulator of Kv3 channels," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    3. Gamma Chi & Qiansheng Liang & Akshay Sridhar & John B. Cowgill & Kasim Sader & Mazdak Radjainia & Pu Qian & Pablo Castro-Hartmann & Shayla Venkaya & Nanki Kaur Singh & Gavin McKinley & Alejandra Ferna, 2022. "Cryo-EM structure of the human Kv3.1 channel reveals gating control by the cytoplasmic T1 domain," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    4. Carlos A. Z. Bassetto & Flavio Costa & Carlo Guardiani & Francisco Bezanilla & Alberto Giacomello, 2023. "Noncanonical electromechanical coupling paths in cardiac hERG potassium channel," Nature Communications, Nature, vol. 14(1), pages 1-11, 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:16:y:2025:i:1:d:10.1038_s41467-025-58443-9. 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.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with 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.