ArticleThe Journal of physiology2005
Molecular mapping of a site for Cd2+-induced modification of human ether-à-go-go-related gene (hERG) channel activation.
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 19 papers, 1 of them a synthesis that pooled it.
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Who cites it
19 citing papers in PubMed, 1 synthesis or guideline pooled it, 27 citations in OpenAlex.
- Calcium and arrhythmogenesis.Physiological reviews · 2007Pooled it
- The voltage-sensing domain of a hERG1 mutant is a cation-selective channel.Biophysical journal · 2022Article
- External Cd2+ and protons activate the hyperpolarization-gated K+ channel KAT1 at the voltage sensor.The Journal of general physiology · 2021Article
- Modulation of hERG KFrontiers in pharmacology · 2020Review
- Identification of a proton sensor that regulates conductance and open time of single hERG channels.Scientific reports · 2019Article
- Extracellular protons accelerate hERG channel deactivation by destabilizing voltage sensor relaxation.The Journal of general physiology · 2019Article
- Molecular Basis of Altered hERG1 Channel Gating Induced by Ginsenoside Rg3.Molecular pharmacology · 2017Article
- Ether-à-go-go family voltage-gated K+ channels evolved in an ancestral metazoan and functionally diversified in a cnidarian-bilaterian ancestor.The Journal of experimental biology · 2015Article
- External protons destabilize the activated voltage sensor in hERG channels.European biophysics journal : EBJ · 2014Article
- Extracellular protons inhibit charge immobilization in the cardiac voltage-gated sodium channel.Biophysical journal · 2013Article
- External pH modulates EAG superfamily K+ channels through EAG-specific acidic residues in the voltage sensor.The Journal of general physiology · 2013Article
- Molecular determinants of pentamidine-induced hERG trafficking inhibition.Molecular pharmacology · 2012Article
- Structural refinement of the hERG1 pore and voltage-sensing domains with ROSETTA-membrane and molecular dynamics simulations.Proteins · 2010Article
- Modification of hERG1 channel gating by Cd2+.The Journal of general physiology · 2010Article
- Divalent cations slow activation of EAG family K+ channels through direct binding to S4.Biophysical journal · 2009Article
- Mechanisms by which atrial fibrillation-associated mutations in the S1 domain of KCNQ1 slow deactivation of IKs channels.The Journal of physiology · 2008Article
- An extracellular Cu2+ binding site in the voltage sensor of BK and Shaker potassium channels.The Journal of general physiology · 2008Article
- Electrostatic domino effect in the Shaker K channel turret.Biophysical journal · 2007Article
- Differences between ion binding to eag and HERG voltage sensors contribute to differential regulation of activation and deactivation gating.Channels (Austin, Tex.)Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Cd(2+) slows the rate of activation, accelerates the rate of deactivation and shifts the half-points of voltage-dependent activation (V(0.5,act)) and inactivation (V(0.5,inact)) of human ether-à-go-go-related gene (hERG) K(+) channels. To identify specific Cd(2+)-binding sites on the hERG channel, we mutated potential Cd(2+)-coordination residues located in the transmembrane domains or extracellular loops linking these domains, including five Cys, three His, nine Asp and eight Glu residues. Each residue was individually substituted with Ala and the resulting mutant channels heterologously expressed in Xenopus oocytes and their biophysical properties determined with standard two-microelectrode voltage-clamp technique. Cd(2+) at 0.5 mM caused a +36 mV shift of V(0.5,act) and a +18 mV shift of V(0.5,inact) in wild-type channels. Most mutant channels had a similar sensitivity to 0.5 mM Cd(2+). Mutation of single Asp residues located in the S2 (D456, D460) or S3 (D509) domains reduced the Cd(2+)-induced shift in V(0.5,act), but not V(0.5,inact). Combined mutations of two or three of these key Asp residues nearly eliminated the shift induced by 0.5 mM Cd(2+). Mutation of D456, D460 and D509 also reduced the comparatively low-affinity effects of Ca(2+) and Mg(2+) on V(0.5,act). Extracellular Cd(2+) modulates hERG channel activation by binding to a coordination site formed, at least in part, by three Asp residues.
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