Evidence map›Paper›PMID 18824591›Full record

ArticleThe Journal of general physiology2008

Gating pore currents in DIIS4 mutations of NaV1.4 associated with periodic paralysis: saturation of ion flux and implications for disease pathogenesis.

Arie F Struyk, Vladislav S Markin, David Francis, Stephen C Cannon

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

55 citing papers in PubMed, 1 synthesis or guideline pooled it, 77 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Therapeutic advances in neurological disorders · 2025
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  5. Article
  6. Article
  7. Pathogenic gating pore current conducted by autism-related mutations in the NaProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Periodic paralysis.Handbook of clinical neurology · 2024
    Review
  9. Article
  10. A TRPM7 mutation linked to familial trigeminal neuralgia: Omega current and hyperexcitability of trigeminal ganglion neurons.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. NaScientific reports · 2018
    Article
  18. Article
  19. Spider toxin inhibits gating pore currents underlying periodic paralysis.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. Stac3 enhances expression of human CaThe Journal of general physiology · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Arie F StruykDepartment of Neurology, University of Texas-Southwestern Medical Center, Dallas, TX 75390, USA. arie.struyk@utsouthwestern.edu
Vladislav S Markin
David Francis
Stephen C Cannon
The University of Texas Southwestern Medical Center · US

Funding

Molecular Physiology of Myotonia and Periodic ParalysisR37AR042703 · NIAMS · UT SOUTHWESTERN MEDICAL CENTER · PI CANNON, STEPHEN C. · 2008 to 2018
$4.2M
MOLECULAR PHYSIOLOGY OF NEUROMUSCULAR DISEASESR01AR042703 · NIAMS · UT SOUTHWESTERN MEDICAL CENTER · PI CANNON, STEPHEN C. · 1994 to 2007
$2.4M
NIAMS NIH HHS R01 AR042703NIAMS NIH HHS R01-AR42703NIAMS NIH HHS R37 AR042703
6 · The paper itself

Abstract

S4 voltage-sensor mutations in CaV1.1 and NaV1.4 channels cause the human muscle disorder hypokalemic periodic paralysis (HypoPP). The mechanism whereby these mutations predispose affected sarcolemma to attacks of sustained depolarization and loss of excitability is poorly understood. Recently, three HypoPP mutations in the domain II S4 segment of NaV1.4 were shown to create accessory ionic permeation pathways, presumably extending through the aqueous gating pore in which the S4 segment resides. However, there are several disparities between reported gating pore currents from different investigators, including differences in ionic selectivity and estimates of current amplitude, which in turn have important implications for the pathological relevance of these aberrant currents. To clarify the features of gating pore currents arising from different DIIS4 mutants, we recorded gating pore currents created by HypoPP missense mutations at position R666 in the rat isoform of Nav1.4 (the second arginine from the outside, at R672 in human NaV1.4). Extensive measurements were made for the index mutation, R666G, which created a gating pore that was permeable to K(+) and Na(+). This current had a markedly shallow slope conductance at hyperpolarized voltages and robust inward rectification, even when the ionic gradient strongly favored outward ionic flow. These characteristics were accounted for by a barrier model incorporating a voltage-gated permeation pathway with a single cation binding site oriented near the external surface of the electrical field. The amplitude of the R666G gating pore current was similar to the amplitude of a previously described proton-selective current flowing through the gating pore in rNaV1.4-R663H mutant channels. Currents with similar amplitude and cation selectivity were also observed in R666S and R666C mutant channels, while a proton-selective current was observed in R666H mutant channels. These results add support to the notion that HypoPP mutations share a common biophysical profile comprised of a low-amplitude inward current at the resting potential that may contribute to the pathological depolarization during attacks of weakness.

Indexed as

Ion Channel GatingAmino Acid SubstitutionAnimalsArginineBinding SitesElectric ConductivityHypokalemic Periodic ParalysisIon TransportMembrane PotentialsModels, MolecularMuscle ProteinsMuscle, SkeletalMutant ProteinsPatch-Clamp TechniquesPotassiumProtonsArginineMuscle ProteinsMutant ProteinsPotassiumProtonsScn4a protein, ratSodiumSodium Channels

Identifiers

PMID18824591
PMCPMC2553391
OpenAlexW2086701162

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.