The neuronal background K2P channels: focus on TREK1
Top Cited Papers
- 1 April 2007
- journal article
- review article
- Published by Springer Nature in Nature Reviews Neuroscience
- Vol. 8 (4) , 251-261
- https://doi.org/10.1038/nrn2117
Abstract
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.Keywords
This publication has 93 references indexed in Scilit:
- AKAP150, a switch to convert mechano-, pH- and arachidonic acid-sensitive TREK K+ channels into open leak channelsThe EMBO Journal, 2006
- TREKing toward new antidepressantsNature Neuroscience, 2006
- TREK-1, a K+ channel involved in polymodal pain perceptionThe EMBO Journal, 2006
- Desensitization of mechano-gated K 2P channelsProceedings of the National Academy of Sciences, 2006
- Sumoylation Silences the Plasma Membrane Leak K+ Channel K2P1Cell, 2005
- Lysophosphatidic Acid-operated K+ ChannelsJournal of Biological Chemistry, 2005
- Forward TransportCell, 2002
- The Structure of the Potassium Channel: Molecular Basis of K + Conduction and SelectivityScience, 1998
- A pH-sensitive Yeast Outward Rectifier K+ Channel with Two Pore Domains and Novel Gating PropertiesJournal of Biological Chemistry, 1996
- Cyclic AMP-dependent protein kinase closes the serotonin-sensitive K+channels of Aplysia sensory neurones in cell-free membrane patchesNature, 1985