ArticleThe Journal of general physiology2003
Molecular motions of the outer ring of charge of the sodium channel: do they couple to slow inactivation?
Article in The Journal of general physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 51 citations in OpenAlex.
- The chemistry of electrical signaling in sodium channels from bacteria and beyond.Cell chemical biology · 2024Review
- P-Loop Channels: Experimental Structures, and Physics-Based and Neural Networks-Based Models.Membranes · 2022Review
- Druggability of Voltage-Gated Sodium Channels-Exploring Old and New Drug Receptor Sites.Frontiers in pharmacology · 2022Review
- Noncanonical Ion Channel Behaviour in Pain.International journal of molecular sciences · 2019Review
- Propofol inhibits prokaryotic voltage-gated NaThe Journal of general physiology · 2018Article
- Eslicarbazepine acetate for the treatment of focal epilepsy: an update on its proposed mechanisms of action.Pharmacology research & perspectives · 2015Review
- A naturally occurring amino acid substitution in the voltage-dependent sodium channel selectivity filter affects channel gating.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2013Article
- Voltage-sensor movements describe slow inactivation of voltage-gated sodium channels I: wild-type skeletal muscle Na(V)1.4.The Journal of general physiology · 2013Article
- Proton sensors in the pore domain of the cardiac voltage-gated sodium channel.The Journal of biological chemistry · 2013Article
- Article
- Gating transitions in the selectivity filter region of a sodium channel are coupled to the domain IV voltage sensor.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Extracellular proton modulation of the cardiac voltage-gated sodium channel, Nav1.5.Biophysical journal · 2011Article
- Inhibition of neuronal voltage-gated sodium channels by brilliant blue G.Molecular pharmacology · 2011Article
- Possible roles of exceptionally conserved residues around the selectivity filters of sodium and calcium channels.The Journal of biological chemistry · 2011Article
- A molecular switch between the outer and the inner vestibules of the voltage-gated Na+ channel.The Journal of biological chemistry · 2010Article
- Dietary cholesterol modulates the excitability of rabbit hippocampal CA1 pyramidal neurons.Neuroscience letters · 2010Article
- Novel molecular determinants in the pore region of sodium channels regulate local anesthetic binding.Molecular pharmacology · 2009Article
- Mechanisms of action of ligands of potential-dependent sodium channels.Neuroscience and behavioral physiology · 2008Article
- Speeding the recovery from ultraslow inactivation of voltage-gated Na+ channels by metal ion binding to the selectivity filter: a foot-on-the-door?Biophysical journal · 2007Article
- Sodium channels: ionic model of slow inactivation and state-dependent drug binding.Biophysical journal · 2007Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In contrast to fast inactivation, the molecular basis of sodium (Na) channel slow inactivation is poorly understood. It has been suggested that structural rearrangements in the outer pore mediate slow inactivation of Na channels similar to C-type inactivation in potassium (K) channels. We probed the role of the outer ring of charge in inactivation gating by paired cysteine mutagenesis in the rat skeletal muscle Na channel (rNav1.4). The outer charged ring residues were substituted with cysteine, paired with cysteine mutants at other positions in the external pore, and coexpressed with rat brain beta1 in Xenopus oocytes. Dithiolthreitol (DTT) markedly increased the current in E403C+E758C double mutant, indicating the spontaneous formation of a disulfide bond and proximity of the alpha carbons of these residues of no more than 7 A. The redox catalyst Cu(II) (1,10-phenanthroline)3 (Cu(phe)3) reduced the peak current of double mutants (E403C+E758C, E403C+D1241C, E403C+D1532C, and D1241C+D1532C) at a rate proportional to the stimulation frequency. Voltage protocols that favored occupancy of slow inactivation states completely prevented Cu(phe)3 modification of outer charged ring paired mutants E403C+E758C, E403C+D1241C, and E403C+D1532C. In contrast, voltage protocols that favored slow inactivation did not prevent Cu(phe)3 modification of other double mutants such as E403C+W756C, E403C+W1239C, and E403C+W1531C. Our data suggest that slow inactivation of the Na channel is associated with a structural rearrangement of the outer ring of charge.
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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.