ArticleProceedings of the National Academy of Sciences of the United States of America1995
Mutation of conserved negatively charged residues in the S2 and S3 transmembrane segments of a mammalian K+ channel selectively modulates channel gating.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 99 citations in OpenAlex.
- Voltage Sensing in Membranes: From Macroscopic Currents to Molecular Motions.The Journal of membrane biology · 2015Review
- Thermodynamic mechanism for the evasion of antibody neutralization in flaviviruses.Journal of the American Chemical Society · 2014Article
- Asymmetric functional contributions of acidic and aromatic side chains in sodium channel voltage-sensor domains.The Journal of general physiology · 2014Article
- Evolutionary imprint of activation: the design principles of VSDs.The Journal of general physiology · 2014Article
- Article
- A gating charge interaction required for late slow inactivation of the bacterial sodium channel NavAb.The Journal of general physiology · 2013Article
- A theoretical model for calculating voltage sensitivity of ion channels and the application on Kv1.2 potassium channel.Biophysical journal · 2012Article
- Functional extension of amino acid triads from the fourth transmembrane segment (S4) into its external linker in Shaker K(+) channels.The Journal of biological chemistry · 2011Article
- Contributions of counter-charge in a potassium channel voltage-sensor domain.Nature chemical biology · 2011Article
- SCN5A mutations associate with arrhythmic dilated cardiomyopathy and commonly localize to the voltage-sensing mechanism.Journal of the American College of Cardiology · 2011Article
- Mechanistic basis for LQT1 caused by S3 mutations in the KCNQ1 subunit of IKs.The Journal of general physiology · 2010Article
- The activated state of a sodium channel voltage sensor in a membrane environment.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Structural determinants of the high affinity extracellular zinc binding site on Cav3.2 T-type calcium channels.The Journal of biological chemistry · 2010Article
- Functional analysis of the Kv1.1 N255D mutation associated with autosomal dominant hypomagnesemia.The Journal of biological chemistry · 2010Article
- Studies of alpha-helicity and intersegmental interactions in voltage-gated Na+ channels: S2D4.PloS one · 2009Article
- Initial response of the potassium channel voltage sensor to a transmembrane potential.Journal of the American Chemical Society · 2009Article
- Structural dynamics of an isolated voltage-sensor domain in a lipid bilayer.Structure (London, England : 1993) · 2008Article
- Acidic residues on the voltage-sensor domain determine the activation of the NaChBac sodium channel.Biophysical journal · 2007Article
- Effects in neocortical neurons of mutations of the Na(v)1.2 Na+ channel causing benign familial neonatal-infantile seizures.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Molecular template for a voltage sensor in a novel K+ channel. I. Identification and functional characterization of KvLm, a voltage-gated K+ channel from Listeria monocytogenes.The Journal of general physiology · 2006Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Voltage-gated channel proteins sense a change in the transmembrane electric field and respond with a conformational change that allows ions to diffuse across the pore-forming structure. Site-specific mutagenesis combined with electrophysiological analysis of expressed mutants in amphibian oocytes has previously established the S4 transmembrane segment as an element of the voltage sensor. Here, we show that mutations of conserved negatively charged residues in S2 and S3 of a brain K+ channel, thought of as countercharges for the positively charged residues in S4, selectively modulate channel gating without modifying the permeation properties. Mutations of Glu235 in S2 that neutralize or reverse charge increase the probability of channel opening and the apparent gating valence. In contrast, replacements of Glu272 by Arg or Thr268 by Asp in S3 decrease the open probability and the apparent gating valence. Residue Glu225 in S2 tolerated replacement only by acidic residues, whereas Asp258 in S3 was intolerant to any attempted change. These results imply that S2 and S3 are unlikely to be involved in channel lining, yet, together with S4, may be additional components of the voltage-sensing structure.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.