ArticleChannels (Austin, Tex.)
Differences between ion binding to eag and HERG voltage sensors contribute to differential regulation of activation and deactivation gating.
Article in Channels (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Metabolic and electrolyte abnormalities as risk factors in drug-induced long QT syndrome.Biophysical reviews · 2022Review
- Modulation of hERG KFrontiers in pharmacology · 2020Review
- Extracellular protons accelerate hERG channel deactivation by destabilizing voltage sensor relaxation.The Journal of general physiology · 2019Article
- Dynamics of the EAG1 KBiochemical and biophysical research communications · 2017Article
- External protons destabilize the activated voltage sensor in hERG channels.European biophysics journal : EBJ · 2014Article
- Tuning of EAG K(+) channel inactivation: molecular determinants of amplification by mutations and a small molecule.The Journal of general physiology · 2012Article
- Voltage-dependent gating of HERG potassium channels.Frontiers in pharmacology · 2012Article
- Modification of hERG1 channel gating by Cd2+.The Journal of general physiology · 2010Article
- Transfer of ion binding site from ether-a-go-go to Shaker: Mg2+ binds to resting state to modulate channel opening.The Journal of general physiology · 2010Article
- S0, where is it?The Journal of general physiology · 2008Article
- Intracellular linkers are involved in Mg2+-dependent modulation of the Eag potassium channel.Channels (Austin, Tex.)Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
HERG (KCNH2) and ether-à-go-go (eag) (KCNH1) are members of the same subfamily of voltage-gated K+ channels. In eag, voltage-dependent activation is significantly slowed by extracellular divalent cations. To exert this effect, ions bind to a site located between transmembrane segments S2 and S3 in the voltage sensor domain where they interact with acidic residues that are conserved only among members of the eag subfamily. In HERG channels, extracellular divalent ions significantly accelerate deactivation. To investigate the ionbinding site in HERG, acidic residues in S2 and S3 were neutralized singly or in pairs to alanine, and the functional effects of extracellular Mg(2+) were characterized in Xenopus oocytes. To modulate deactivation kinetics in HERG, divalent cations interact with eag subfamily-specific acidic residues (D460 and D509) and also with an acidic residue in S2 (D456) that is widely conserved in the voltage-gated channel superfamily. In contrast, the analogous widely-conserved residue does not contribute to the ion-binding site that modulates activation kinetics in eag. We propose that structural differences between the ion-binding sites in the eag and HERG voltage sensors contribute to the differential regulation of activation and deactivation gating in these channels. A previously proposed model for S4 conformational changes during voltagedependent activation can account for the differential regulation of gating seen in eag and HERG.
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