Two-pore domain K+ (K2P) channels give rise to leak (also called background) K+ currents. The well-known role of background K+ currents is to stabilize the negative resting membrane potential and c...

/pdf/molecular-background-of-leak-k-currents-two-pore-domain-3xd1km54it.pdf

Molecular Background of Leak K+ Currents: Two-Pore Domain Potassium Channels

In less than a decade since their discovery, the study of K2P channels has revealed that background leak of potassium ions via dedicated pathways is a highly regulated mechanism to control cellular excitability. Potassium leak pathways, active at rest, stabilize membrane potential below firing

/pdf/international-union-of-pharmacology-lv-nomenclature-and-3e6n6k9ffb.pdf

International Union of Pharmacology. LV. Nomenclature and Molecular Relationships of Two-P Potassium Channels

Objective: The biophysical properties and the regulation of the two-pore-domain potassium channel TREK-1 were studied in rat cardiomyocytes. Methods: RT-PCR, immunohistochemistry and patch-clamp recording were performed in isolated rat ventricular cardiomyocytes. In some whole-cell-clamp experiments the myocytes were mechanically stretched using a glass stylus. Results: We found strong expression of a splice variant of TREK-1 in rat heart. Immunohistochemistry with antibodies against TREK-1 showed localization of the channel in longitudinal stripes at the external surface membrane of cardiomyocytes. When the cardiomyocytes were mechanically stretched, an outwardly rectifying K + current component could be detected in whole-cell recordings. In single-channel recordings with symmetrical high K + solution, two TREK-like channels with Fflickery-burst_ kinetics were found: a Flarge conductance_ K + channel (132 T5 pS at positive potentials) and a novel Flow-conductance_ channel (41 T5 pS at positive potentials). The low-conductance channel could be activated by negative pressure in inside-out patches, positive pressure in outside-out patches, intracellular acidification and application of arachidonic acid. Its open probability was strongly increased by depolarization, due to decreased duration of gaps between bursts. The biophysical properties of the two cardiac TREK-like channels were similar to those of TREK-1 channels expressed in HEK293 cells, which both displayed low- and high-conductance modes. Conclusions: Our results suggest that the two TREK-like channels found in rat cardiomyocytes may reflect two different operating modes of TREK-1. The novel low-conductance channels described here may represent the major operating mode of TREK-1. The current flowing through mechanogated TREK-1 channels may serve to counterbalance the inward current flowing through stretch-activated non-selective cation channels during the filling phase of the cardiac cycle and thus to prevent the occurrence of ventricular extrasystoles.

/pdf/the-stretch-activated-potassium-channel-trek-1-in-rat-1hsgtytouq.pdf

The stretch-activated potassium channel TREK-1 in rat cardiac ventricular muscle

Basic Concepts Electricity, nerves, batteries: A short history Clay M. Armstrong Ion selectivity and conductance Dorothy M. Kim, Jason G. McCoy, and Crina M. Nimigean Basic mechanisms of voltage sensing Sandipan Chowdhury and Baron Chanda Ligand-dependent gating mechanism William N. Zagotta Mechanosensitive channels and their emerging gating mechanisms Sergei Sukharev and Andriy Anishkin Ion Channel Methods Patch clamping and single-channel analysis Leon D. Islas Models of ion channel gating Frank T. Horrigan and Toshinori Hoshi Utilizing Markov chains to model ion channel sequence variation and kinetics Anthony Fodor Investigation of ion channel structure using fluorescence spectroscopy Rikard Blunck A practical guide to solving the structure of an ion channel protein Tahmina Rahman and Declan A. Doyle Structural study of ion channels by cryo-electron microscopy Qiu-Xing Jiang and Liang Shi Rosetta structural modeling Vladimir Yarov-Yarovoy Genetic methods for studying ion channel function in physiology and disease Andrea L. Meredith Ion channel inhibitors Jon Sack and Kenneth S. Eum High-throughput methods for ion channels Haibo Yu and Min Li Ion Channel Families Voltage-gated sodium channels William A. Catterall BK channels Huanghe Yang and Jianmin Cui Inward rectifying potassium channels Monica Sala-Rabanal and Colin G. Nichols Two-pore domain potassium channels Leigh D. Plant and Steve A.N. Goldstein KCNQ channels Nikita Gamper and Mark S. Shapiro Ionotropic glutamate receptors Andrew Plested 5-HT3 receptors Sarah C.R. Lummis GABAA receptors Trevor G. Smart Cyclic nucleotide-gated channels Michael D. Varnum and Gucan Dai Acid-sensing ion channels Cecilia Canessa Degenerin/ENaC channels James D. Stockand TRPC channels Jin-Bin Tian, Dhananjay Thakur, Yungang Lu, and Michael X. Zhu TRPV channels Sharona E. Gordon TRPM channels David D. McKemy TRPML channels Qiong Gao, Xiaoli Zhang, and Haoxing Xu CLC chloride channels and transporters Giovanni Zifarelli and Michael Pusch Ca-activated chloride channels Xiuming Wong and Lily Jan Store-operated CRAC channels Murali Prakriya Ion Channel Regulation Mechanism of G-protein regulation of K+ channels Rahul Mahajan and Diomedes E. Logothetis Calmodulin regulation of voltage-gated calcium channels and beyond Manu Ben-Johny and David T. Yue Phosphorylation of voltage-gated ion channels James S. Trimmer and Hiroaki Misonou Alternative splicing Andrea L. Meredith Single transmembrane regulatory subunits of voltage-gated potassium channels William R. Kobertz and Anatoli Lvov Ion Channel Physiology and Diseases Ion channels of the heart Donald M. Bers and Eleonora Grandi Ion channels in pain J.P. Johnson, Jr. CLC-related proteins in diseases Allan H. Bretag and Linlin Ma Cystic fibrosis and the CFTR anion channel Yoshiro Sohma and Tzyh-Chang Hwang Drugs targeting ion channels KeWei Wang Index

Handbook of ion channels

GABAB Receptor Activation Inhibits Neuronal Excitability and Spatial Learning in the Entorhinal Cortex by Activating TREK-2 K+ Channels

Functional expression of TRESK-2, a new member of the tandem-pore K+ channel family.

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Functional expression of TRESK-2, a new member of the tandem-pore K+ channel family.