Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals

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Author(s)

Abstract

<p>The voltage sensor domain (VSD) has long been studied as a unique domain intrinsic to voltage-gated ion channels (VGICs). Within VGICs, the VSD is tightly coupled to the pore-gate domain (PGD) in diverse ways suitable for its specific function in each physiological context, including action potential generation, muscle contraction and relaxation, hormone and neurotransmitter secretion, and cardiac pacemaking. However, some VSD-containing proteins lack a PGD. Voltage-sensing phosphatase contains a cytoplasmic phosphoinositide phosphatase with similarity to phosphatase and tensin homolog (PTEN). H<sub>v</sub>1, a voltage-gated proton channel, also lacks a PGD. Within H<sub>v</sub>1, the VSD operates as a voltage sensor, gate, and pore for both proton sensing and permeation. H<sub>v</sub>1 has a C-terminal coiled coil that mediates dimerization for cooperative gating. Recent progress in the structural biology of VGICs and VSD proteins provides insights into the principles of VSD coupling conserved among these proteins as well as the hierarchy of protein organization for voltage-evoked cell signaling.</p>

Journal

  • Proceedings of the Japan Academy, Series B

    Proceedings of the Japan Academy, Series B 95(3), 111-135, 2019

    The Japan Academy

Codes

  • NII Article ID (NAID)
    130007610041
  • NII NACSIS-CAT ID (NCID)
    AA00785485
  • Text Lang
    ENG
  • ISSN
    0386-2208
  • NDL Article ID
    029596126
  • NDL Call No.
    Z53-T495
  • Data Source
    NDL  J-STAGE 
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