ArticleThe Journal of physiology2001
GYGD pore motifs in neighbouring potassium channel subunits interact to determine ion selectivity.
Article in The Journal of physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 48 citations in OpenAlex.
- Distinct mechanisms of inhibition of Kv2 potassium channels by tetraethylammonium and RY785.eLife · 2026Article
- Investigation of two-pore KHeliyon · 2024Article
- Nine patients with KCNQ2-related neonatal seizures and functional studies of two missense variants.Scientific reports · 2023Article
- New Insights into Plant TPK Ion Channel Evolution.Plants (Basel, Switzerland) · 2021Article
- Unraveling of a Strongly Correlated Dynamical Network of Residues Controlling the Permeation of Potassium in KcsA Ion Channel.Entropy (Basel, Switzerland) · 2021Article
- The Selectivity Filter Is Involved in the U-Type Inactivation Process of Kv2.1 and Kv3.1 Channels.Biophysical journal · 2020Article
- Localization-dependent activity of the Kv2.1 delayed-rectifier K+ channel.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Developmental expression of a functional TASK-1 2P domain K+ channel in embryonic chick heart.Journal of biomedical science · 2009Article
- Functional consequences of leucine and tyrosine mutations in the dual pore motifs of the yeast K(+) channel, Tok1p.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
- Ion conductance vs. pore gating and selectivity in KcsA channel: modeling achievements and perspectives.Journal of molecular modeling · 2007Article
- Channel-mediated potassium uptake in Helicobacter pylori is essential for gastric colonization.The EMBO journal · 2007Article
- Control of single channel conductance in the outer vestibule of the Kv2.1 potassium channel.The Journal of general physiology · 2006Article
- Allosteric effects of external K+ ions mediated by the aspartate of the GYGD signature sequence in the Kv2.1 K+ channel.Pflugers Archiv : European journal of physiology · 2006Article
- pH sensing in the two-pore domain K+ channel, TASK2.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- K channel subconductance levels result from heteromeric pore conformations.The Journal of general physiology · 2005Article
- Selectivity and interactions of Ba2+ and Cs+ with wild-type and mutant TASK1 K+ channels expressed in Xenopus oocytes.The Journal of physiology · 2005Article
- Regulation of K+ flow by a ring of negative charges in the outer pore of BKCa channels. Part II: Neutralization of aspartate 292 reduces long channel openings and gating current slow component.The Journal of general physiology · 2004Article
- Regulation of K+ flow by a ring of negative charges in the outer pore of BKCa channels. Part I: Aspartate 292 modulates K+ conduction by external surface charge effect.The Journal of general physiology · 2004Article
- The selectivity filter of the tandem pore potassium channel TASK-1 and its pH-sensitivity and ionic selectivity.Pflugers Archiv : European journal of physiology · 2004Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Cells maintain a negative resting membrane potential through the constitutive activity of background K+ channels. A novel multigene family of such K+ channels has recently been identified. A unique characteristic of these K+ channels is the presence of two homologous, subunit-like domains, each containing a pore-forming region. Sequence co-variations in the GYGD signature motifs of the two pore regions suggested an interaction between neighbouring pore domains. Mutations of the GYGD motif in the rat drk1 (Kv2.1) K+ channel showed that the tyrosine (Y) position was important for K+ selectivity and single channel conductance, whereas the aspartate (D) position was a critical determinant of open state stability. Tandem constructs engineered to mimic the GYGx-GxGD pattern seen in two-domain K+ channels delineated a co-operative intersubunit interaction between the Y and D positions, which determined ion selectivity, conductance and gating. In the bacterial KcsA K+ channel crystal structure, the equivalent aspartate residue (D80) does not directly interact with permeating K+ ions. However, the data presented here show that the D position is able to fine-tune ion selectivity through a functional interaction with the Y position in the neighbouring subunit. These data indicate a physiological basis for the extensive sequence variation seen in the GYGD motifs of two-domain K+ channels. It is suggested that a cell can precisely regulate its resting membrane potential by selectively expressing a complement of two-domain K+ channels.
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