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Molecular basis of the voltage-dependent gating of TREK-1, a mechano-sensitive K(+) channel

François Maingret1, Eric Honoré, Michel Lazdunski

  • 1Institut de Pharmacologie Moléculaire et Cellulaire, CNRS, UMR 6097, Sophia Antipolis, Valbonne, France.

Biochemical and Biophysical Research Communications
|March 22, 2002
PubMed

Insights

TREK-1 potassium channels exhibit voltage-dependent gating and Mg2+ block at negative potentials. The carboxy terminal domain controls this gating, impacting neuronal firing and action potential duration.

Area of Science:

  • Molecular Biology
  • Neuroscience
  • Ion Channel Physiology

Background:

  • TREK-1 belongs to the mammalian two P domain potassium channel family.
  • TREK-1 channels play roles in neuronal excitability and pain signaling.

Purpose of the Study:

  • To investigate the molecular mechanisms underlying TREK-1 channel gating.
  • To identify the regions of TREK-1 responsible for voltage-dependent gating and its functional consequences.

Main Methods:

  • Transient transfection of COS cells with TREK-1 constructs.
  • Electrophysiological recordings to assess channel activity.
  • Deletional and chimeric analysis to map functional domains.

Main Results:

  • TREK-1 activity is reduced at negative membrane potentials by Mg2+ block and intrinsic voltage-dependent gating.
  • A strong outward rectification is observed in TREK-1.
  • The carboxy terminal domain, not the S333 PKA site, mediates voltage-dependent gating.
  • The carboxy terminal domain is also crucial for TREK-1 mechano-gating, suggesting a functional link.

Conclusions:

  • TREK-1 voltage-dependent gating is primarily mediated by its carboxy terminal domain.
  • This gating mechanism, potentially linked to mechano-gating, influences neuronal firing properties.
  • Understanding TREK-1 gating is vital for comprehending neuronal excitability and action potential dynamics.

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