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Steric hindrance between S4 and S5 of the KCNQ1/KCNE1 channel hampers pore opening

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  • Koichi Nakajo

    (National Institute for Physiological Sciences
    Department of Physiological Sciences)

  • Yoshihiro Kubo

    (National Institute for Physiological Sciences
    Department of Physiological Sciences)

Abstract

In voltage-gated K+ channels, membrane depolarization induces an upward movement of the voltage-sensing domains (VSD) that triggers pore opening. KCNQ1 is a voltage-gated K+ channel and its gating behaviour is substantially modulated by auxiliary subunit KCNE proteins. KCNE1, for example, markedly shifts the voltage dependence of KCNQ1 towards the positive direction and slows down the activation kinetics. Here we identify two phenylalanine residues on KCNQ1, Phe232 on S4 (VSD) and Phe279 on S5 (pore domain) to be responsible for the gating modulation by KCNE1. Phe232 collides with Phe279 during the course of the VSD movement and hinders KCNQ1 channel from opening in the presence of KCNE1. This steric hindrance caused by the bulky amino-acid residues destabilizes the open state and thus shifts the voltage dependence of KCNQ1/KCNE1 channel.

Suggested Citation

  • Koichi Nakajo & Yoshihiro Kubo, 2014. "Steric hindrance between S4 and S5 of the KCNQ1/KCNE1 channel hampers pore opening," Nature Communications, Nature, vol. 5(1), pages 1-11, September.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5100
    DOI: 10.1038/ncomms5100
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    Cited by:

    1. Georg Kuenze & Amanda M Duran & Hope Woods & Kathryn R Brewer & Eli Fritz McDonald & Carlos G Vanoye & Alfred L George Jr. & Charles R Sanders & Jens Meiler, 2019. "Upgraded molecular models of the human KCNQ1 potassium channel," PLOS ONE, Public Library of Science, vol. 14(9), pages 1-33, September.

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