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The twisted ion-permeation pathway of a resting voltage-sensing domain

Author

Listed:
  • Francesco Tombola

    (University of California)

  • Medha M. Pathak

    (University of California
    Harvard Medical School)

  • Pau Gorostiza

    (University of California
    Center of Bioengineering of Catalonia (CREBEC))

  • Ehud Y. Isacoff

    (University of California
    Lawrence Berkeley National Laboratory)

Abstract

Proteins containing voltage-sensing domains (VSDs) translate changes in membrane potential into changes in ion permeability or enzymatic activity1,2,3. In channels, voltage change triggers a switch in conformation of the VSD, which drives gating in a separate pore domain, or, in channels lacking a pore domain, directly gates an ion pathway within the VSD4,5. Neither mechanism is well understood6. In the Shaker potassium channel, mutation of the first arginine residue of the S4 helix to a smaller uncharged residue makes the VSD permeable to ions (‘omega current’) in the resting conformation (‘S4 down’)7. Here we perform a structure-guided perturbation analysis of the omega conductance to map its VSD permeation pathway. We find that there are four omega pores per channel, which is consistent with one conduction path per VSD. Permeating ions from the extracellular medium enter the VSD at its peripheral junction with the pore domain, and then plunge into the core of the VSD in a curved conduction pathway. Our results provide a model of the resting conformation of the VSD.

Suggested Citation

  • Francesco Tombola & Medha M. Pathak & Pau Gorostiza & Ehud Y. Isacoff, 2007. "The twisted ion-permeation pathway of a resting voltage-sensing domain," Nature, Nature, vol. 445(7127), pages 546-549, February.
    • Handle: RePEc:nat:nature:v:445:y:2007:i:7127:d:10.1038_nature05396
    DOI: 10.1038/nature05396
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    Cited by:

    1. Chang Zhao & Parker D. Webster & Alexis Angeli & Francesco Tombola, 2023. "Mechanically-primed voltage-gated proton channels from angiosperm plants," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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