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The Electrically Silent Kv6.4 Subunit Confers Hyperpolarized Gating Charge Movement in Kv2.1/Kv6.4 Heterotetrameric Channels

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  • Elke Bocksteins
  • Alain J Labro
  • Dirk J Snyders
  • Durga P Mohapatra

Abstract

The voltage-gated K+ (Kv) channel subunit Kv6.4 does not form functional homotetrameric channels but co-assembles with Kv2.1 to form functional Kv2.1/Kv6.4 heterotetrameric channels. Compared to Kv2.1 homotetramers, Kv6.4 exerts a ∼40 mV hyperpolarizing shift in the voltage-dependence of Kv2.1/Kv6.4 channel inactivation, without a significant effect on activation gating. However, the underlying mechanism of this Kv6.4-induced modulation of Kv2.1 channel inactivation, and whether the Kv6.4 subunit participates in the voltage-dependent gating of heterotetrameric channels is not well understood. Here we report distinct gating charge movement of Kv2.1/Kv6.4 heterotetrameric channels, compared to Kv2.1 homotetramers, as revealed by gating current recordings from mammalian cells expressing these channels. The gating charge movement of Kv2.1/Kv6.4 heterotetrameric channels displayed an extra component around the physiological K+ equilibrium potential, characterized by a second sigmoidal relationship of the voltage-dependence of gating charge movement. This distinct gating charge displacement reflects movement of the Kv6.4 voltage-sensing domain and has a voltage-dependency that matches the hyperpolarizing shift in Kv2.1/Kv6.4 channel inactivation. These results provide a mechanistic basis for the modulation of Kv2.1 channel inactivation gating kinetics by silent Kv6.4 subunits.

Suggested Citation

  • Elke Bocksteins & Alain J Labro & Dirk J Snyders & Durga P Mohapatra, 2012. "The Electrically Silent Kv6.4 Subunit Confers Hyperpolarized Gating Charge Movement in Kv2.1/Kv6.4 Heterotetrameric Channels," PLOS ONE, Public Library of Science, vol. 7(5), pages 1-7, May.
    • Handle: RePEc:plo:pone00:0037143
    DOI: 10.1371/journal.pone.0037143
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    Cited by:

    1. Jeroen I Stas & Elke Bocksteins & Alain J Labro & Dirk J Snyders, 2015. "Modulation of Closed−State Inactivation in Kv2.1/Kv6.4 Heterotetramers as Mechanism for 4−AP Induced Potentiation," PLOS ONE, Public Library of Science, vol. 10(10), pages 1-21, October.

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