title: Lipid and mechano-gated 2P domain K(+) channels.
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.
authors.affiliation: Institut de Pharmacologie Moléculaire et Cellulaire, CNRS-UMR 6097, 660 route des Lucioles, Sophia Antipolis, 06560, Valbonne, France.
authors.forename: A J
authors.initials: AJ
authors.lastname: Patel
authors.forename: M
authors.initials: M
authors.lastname: Lazdunski
authors.forename: E
authors.initials: E
authors.lastname: Honoré
mesh_terms: D000818:Animals; D005231:Fatty Acids, Unsaturated / Q000502:physiology*; D015640:Ion Channel Gating; D008246:Lysophospholipids / Q000502:physiology*; D015221:Potassium Channels / Q000378:metabolism / Q000502:physiology*; D024683:Potassium Channels, Tandem Pore Domain; D013314:Stress, Mechanical
chemical_list: D005231:Fatty Acids, Unsaturated; D008246:Lysophospholipids; D015221:Potassium Channels; D024683:Potassium Channels, Tandem Pore Domain; C103742:potassium channel protein TREK-1