title: The mechano-gated K(2P) channel TREK-1.
abstract: 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.
authors: Institut de Pharmacologie Moléculaire et Cellulaire, CNRS UMR 6097, Université de Nice-Sophia Antipolis, 660 route des Lucioles, 06560 Valbonne, France.
authors: Alexandra
authors: A
authors: Dedman
authors: Reza
authors: R
authors: Sharif-Naeini
authors: Joost H A
authors: JH
authors: Folgering
authors: Fabrice
authors: F
authors: Duprat
authors: Amanda
authors: A
authors: Patel
authors: Eric
authors: E
authors: Honoré
mesh_terms: D000818:Animals; D005231:Fatty Acids, Unsaturated / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D015640:Ion Channel Gating / Q000502:physiology; D008563:Membrane Lipids / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism; D024683:Potassium Channels, Tandem Pore Domain / Q000502:physiology*; D043562:Receptors, G-Protein-Coupled / Q000502:physiology; D015290:Second Messenger Systems / Q000502:physiology; D013314:Stress, Mechanical; D013696:Temperature
chemical_list: D005231:Fatty Acids, Unsaturated; D008563:Membrane Lipids; D010743:Phospholipids; D024683:Potassium Channels, Tandem Pore Domain; D043562:Receptors, G-Protein-Coupled; C103742:potassium channel protein TREK-1