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

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

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Institut de Pharmacologie Moléculaire et Cellulaire, CNRS UMR 6097, Université de Nice-Sophia Antipolis, 660 route des Lucioles, 06560 Valbonne, France.


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.

[Indexed for MEDLINE]

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