The mechano-gated K(2P) channel TREK-1

Eur Biophys J. 2009 Mar;38(3):293-303. doi: 10.1007/s00249-008-0318-8. Epub 2008 Mar 28.


The versatility of neuronal electrical activity is largely conditioned by the expression of different structural and functional classes of K+ channels. More than 80 genes encoding the main K+ channel alpha subunits have been identified in the human genome. Alternative splicing, heteromultimeric assembly, post-translational modification and interaction with auxiliary regulatory subunits further increase the molecular and functional diversity of K+ channels. Mammalian two-pore domain K+ channels (K(2P)) make up one class of K+ channels along with the inward rectifiers and the voltage- and/or calcium-dependent K+ channels. Each K(2P) channel subunit is made up of four transmembrane segments and two pore-forming (P) domains, which are arranged in tandem and function as either homo- or heterodimeric channels. This novel structural arrangement is associated with unusual gating properties including "background" or "leak" K+ channel activity, in which the channels show constitutive activity at rest. In this review article, we will focus on the lipid-sensitive mechano-gated K(2P) channel TREK-1 and will emphasize on the polymodal function of this "unconventional" K+ channel.

Publication types

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

MeSH terms

  • Animals
  • Fatty Acids, Unsaturated / metabolism
  • Humans
  • Hydrogen-Ion Concentration
  • Ion Channel Gating / physiology
  • Membrane Lipids / metabolism
  • Phospholipids / metabolism
  • Potassium Channels, Tandem Pore Domain / physiology*
  • Receptors, G-Protein-Coupled / physiology
  • Second Messenger Systems / physiology
  • Stress, Mechanical
  • Temperature


  • Fatty Acids, Unsaturated
  • Membrane Lipids
  • Phospholipids
  • Potassium Channels, Tandem Pore Domain
  • Receptors, G-Protein-Coupled
  • potassium channel protein TREK-1