ArticleThe Journal of physiology2005
Selectivity and interactions of Ba2+ and Cs+ with wild-type and mutant TASK1 K+ channels expressed in Xenopus oocytes.
Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Structure-Function Relationships of KAdvances in experimental medicine and biology · 2026Review
- Advances in the Understanding of Two-Pore Domain TASK Potassium Channels and Their Potential as Therapeutic Targets.Molecules (Basel, Switzerland) · 2022Review
- Potassium channel dysfunction underlies Purkinje neuron spiking abnormalities in spinocerebellar ataxia type 2.Human molecular genetics · 2017Article
- The isoforms generated by alternative translation initiation adopt similar conformation in the selectivity filter in TREK-2.Journal of physiology and biochemistry · 2015Article
- Acid-sensitive TWIK and TASK two-pore domain potassium channels change ion selectivity and become permeable to sodium in extracellular acidification.The Journal of biological chemistry · 2012Article
- External Ba2+ block of the two-pore domain potassium channel TREK-1 defines conformational transition in its selectivity filter.The Journal of biological chemistry · 2011Article
- Two-pore domain K⁺ channels regulate membrane potential of isolated human articular chondrocytes.The Journal of physiology · 2011Article
- Endothelial and smooth muscle cell ion channels in pulmonary vasoconstriction and vascular remodeling.Comprehensive Physiology · 2011Review
- Intrinsic membrane properties of locus coeruleus neurons in Mecp2-null mice.American journal of physiology. Cell physiology · 2010Article
- Gating the pore of potassium leak channels.European biophysics journal : EBJ · 2009Review
- TRESK-like potassium channels in leukemic T cells.Pflugers Archiv : European journal of physiology · 2008Article
- The selectivity, voltage-dependence and acid sensitivity of the tandem pore potassium channel TASK-1: contributions of the pore domains.Pflugers Archiv : European journal of physiology · 2007Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The acid-sensitive K(+) channel, TASK1 is a member of the K(+)-selective tandem-pore domain (K2P) channel family. Like many of the K2P channels, TASK1 is relatively insensitive to conventional channel blockers such as Ba(2+). In this paper we report the impact of mutating the pore-neighbouring histidine residues, which are involved in pH sensing, on the sensitivity to blockade by Ba(2+) and Cs(+); additionally we compare the selectivity of these channels to extracellular K(+), Na(+) and Rb(+). H98D and H98N mutants showed reduced selectivity for K(+) over both Na(+) and Rb(+), and significant permeation of Rb(+). This enhanced permeability must reflect changes in the structure or flexibility of the selectivity filter. Blockade by Ba(2+) and Cs(+) was voltage-dependent, indicating that both ions block within the pore. In 100 mm K(+), the K(D) at 0 mV for Ba(2+) was 36 +/- 10 mm (n = 6), whilst for Cs(+) it was 20 +/- 6.0 mm (n = 5). H98D was more sensitive to Ba(2+) than the wild-type (WT); in addition, the site at which Ba(2+) appears to bind was altered (WT: delta, 0.64 +/- 0.16, n = 6; H98D: delta, 0.16 +/- 0.03, n = 5, statistically different from WT; H98N: delta, 0.58 +/- 0.09, not statistically different from WT). Thus, the pore-neighbouring residue H98 contributes not only to the pH sensitivity of TASK1, but also to the structure of the conduction pathway.
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Registered trials
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