Lipid and mechano-gated 2P domain K(+) channels

Curr Opin Cell Biol. 2001 Aug;13(4):422-8. doi: 10.1016/s0955-0674(00)00231-3.

Abstract

The two pore domain K(+) channels TREK and TRAAK are opened by membrane stretch. The activating mechanical force comes from the bilayer membrane and is independent of the cytoskeleton. Emerging work shows that mechano-gated TREK and TRAAK are opened by various lipids, including long chain polyunsaturated anionic fatty acids and neutral cone-shaped lysophospholipids. TREK-1 shares the properties of the Aplysia neuronal S channel, a presynaptic background K(+) channel involved in behavioral sensitization, a simple form of learning.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Fatty Acids, Unsaturated / physiology*
  • Ion Channel Gating
  • Lysophospholipids / physiology*
  • Potassium Channels / metabolism
  • Potassium Channels / physiology*
  • Potassium Channels, Tandem Pore Domain*
  • Stress, Mechanical

Substances

  • Fatty Acids, Unsaturated
  • Lysophospholipids
  • Potassium Channels
  • Potassium Channels, Tandem Pore Domain
  • potassium channel protein TREK-1