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Gating of two pore domain potassium channels

Mathie, Alistair, Al-Moubarak, Ehab, Veale, Emma L. (2010) Gating of two pore domain potassium channels. Journal of Physiology, 588 . pp. 3149-3156. ISSN 0022-3751. (doi:10.1113/jphysiol.2010.192344) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1113/jphysiol.2010.192344

Abstract

Two-pore-domain potassium (K2P) channels are responsible for background leak currents which regulate the membrane potential and excitability of many cell types. Their activity is modulated by a variety of chemical and physical stimuli which act to increase or decrease the open probability of individual K2P channels. Crystallographic data and homology modelling suggest that all K(+) channels possess a highly conserved structure for ion selectivity and gating mechanisms. Like other K(+) channels, K2P channels are thought to have two primary conserved gating mechanisms: an inactivation (or C-type) gate at the selectivity filter close to the extracellular side of the channel and an activation gate at the intracellular entrance to the channel involving key, identified, hinge glycine residues. Zinc and hydrogen ions regulate Drosophila KCNK0 and mammalian TASK channels, respectively, by interacting with the inactivation gate of these channels. In contrast, the voltage dependence of TASK3 channels is mediated through its activation gate. For KCNK0 it has been shown that the gates display positive cooperativity. It is of much interest to determine whether other K2P regulatory compounds interact with either the activation gate or the inactivation gate to alter channel activity or, indeed, whether additional regulatory gating pathways exist.

Item Type: Article
DOI/Identification number: 10.1113/jphysiol.2010.192344
Subjects: Q Science > QP Physiology (Living systems)
Divisions: Faculties > Sciences > Medway School of Pharmacy
Depositing User: Alistair Mathie
Date Deposited: 06 Mar 2014 17:04 UTC
Last Modified: 10 Jun 2019 14:51 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/38624 (The current URI for this page, for reference purposes)
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