The neuronal background K2P channels: focus on TREK1.
Two-pore-domain K(+) (K(2P)) channel subunits are made up of four transmembrane segments and two pore-forming domains that are arranged in tandem and function as either homo- or heterodimeric channels. This structural motif is associated with unusual gating properties, including background channel activity and sensitivity to membrane stretch. Moreover, K(2P) channels are modulated by a variety of cellular lipids and pharmacological agents, including polyunsaturated fatty acids and volatile general anaesthetics. Recent in vivo studies have demonstrated that TREK1, the most thoroughly studied K(2P) channel, has a key role in the cellular mechanisms of neuroprotection, anaesthesia, pain and depression.
Honoré
Eric
E
Institut de Pharmacologie Moléculaire et Cellulaire, CNRS UMR 6097, Université de Nice-Sophia Antipolis, 660 route des Lucioles, 06560 Valbonne, France. honore@ipmc.cnrs.fr
D000777:Anesthetics / Q000494:pharmacology; D000818:Animals; D006801:Humans; D018696:Neuroprotective Agents / Q000494:pharmacology; D010146:Pain / Q000503:physiopathology; D024683:Potassium Channels, Tandem Pore Domain / Q000187:drug effects / Q000235:genetics / Q000502:physiology*
D000777:Anesthetics; D018696:Neuroprotective Agents; D024683:Potassium Channels, Tandem Pore Domain; C103742:potassium channel protein TREK-1