ArticleBiophysical journal2002
Outer and central charged residues in DIVS4 of skeletal muscle sodium channels have differing roles in deactivation.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- NaBiophysical journal · 2021Review
- A perspective on Na and K channel inactivation.The Journal of general physiology · 2018Review
- Defective fast inactivation recovery of Nav 1.4 in congenital myasthenic syndrome.Annals of neurology · 2015Article
- Differential state-dependent modification of inactivation-deficient Nav1.6 sodium channels by the pyrethroid insecticides S-bioallethrin, tefluthrin and deltamethrin.Neurotoxicology · 2012Article
- Charge immobilization of skeletal muscle Na+ channels: role of residues in the inactivation linker.Biophysical journal · 2007Article
- Central charged residues in DIIIS4 regulate deactivation gating in skeletal muscle sodium channels.Cellular and molecular neurobiology · 2007Article
- Single-channel properties of human NaV1.1 and mechanism of channel dysfunction in SCN1A-associated epilepsy.The Journal of general physiology · 2006Article
- K-aggravated myotonia mutations at residue G1306 differentially alter deactivation gating of human skeletal muscle sodium channels.Cellular and molecular neurobiology · 2005Article
- Functional characterization and cold sensitivity of T1313A, a new mutation of the skeletal muscle sodium channel causing paramyotonia congenita in humans.The Journal of physiology · 2004Article
- Gating properties of a sodium channel with three arginines substituted by histidines in the central part of voltage sensor S4D4.The Journal of membrane biology · 2003Article
- Negative charges in the DIII-DIV linker of human skeletal muscle Na+ channels regulate deactivation gating.The Journal of physiology · 2003Article
- Open- and closed-state fast inactivation in sodium channels: differential effects of a site-3 anemone toxin.Channels (Austin, Tex.)Article
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Authors and funding
4 authors.
Funding
Abstract
We tested the effects of charge-neutralizing mutations of the eight arginine residues in DIVS4 of the rat skeletal muscle sodium channel (rNa(V)1.4) on deactivation gating from the open and inactivated states. We hypothesized that neutralization of outer or central charges would accelerate the I-to-C transition as measured by recovery delay because these represent a portion of the immobilizable charge. R1Q abbreviated recovery delay as a consequence of reduced charge content. R4Q increased delay, whereas R5Q abbreviated delay, and charge-substitutions at these residues indicated that each effect was allosteric. We also hypothesized that neutralization of any residue in DIVS4 would slow the O-to-C transition with reduction in positive charge. Reduction in charge at R1, and to a lesser extent at R5, slowed open-state deactivation, while charge neutralizations at R2, R3, R4, R6, and R7 accelerated open-state deactivation. Our findings suggest that arginine residues in DIVS4 in rNa(V)1.4 have differing roles in channel closure from open and inactivated states. Furthermore, they suggest that deactivation in DIVS4 is regulated by charge interaction between the electrical field with the outermost residue, and by local allosteric interactions imparted by central charges.
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