Evidence map›Paper›PMID 36292983›Full record

ArticleInternational journal of molecular sciences2022

Genetic Variant in Nicotinic Receptor α4-Subunit Causes Sleep-Related Hyperkinetic Epilepsy via Increased Channel Opening.

Simone Mazzaferro, Deborah J Msekela, Edward C Cooper, Atul Maheshwari, Steven M Sine

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. 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

5 authors at 2 institutions in 1 country.

Simone MazzaferroDepartments of Physiology and Biomedical Engineering, Mayo Clinic College of Medicine and Science, Rochester, MN 55905, USA.
Deborah J MsekelaDepartments of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic College of Medicine and Science, Rochester, MN 55905, USA.
Edward C CooperDepartment of Neurology, Baylor College of Medicine, Houston, TX 77030, USA.
Atul MaheshwariDepartment of Neurology, Baylor College of Medicine, Houston, TX 77030, USA.
Steven M SineDepartments of Physiology and Biomedical Engineering, Mayo Clinic College of Medicine and Science, Rochester, MN 55905, USA.
Mayo Clinic · USBaylor College of Medicine · US

Funding

Project 3 - Development and investigation of murine models of channelopathy-associated epilepsyU54NS108874 · NINDS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI VANOYE, CARLOS G. · 2018 to 2022
$12.1M
STRUCTURE/FUNCTION OF THE ACETYLCHOLINE RECEPTORR01NS031744 · NINDS · MAYO CLINIC ROCHESTER · PI SINE, STEVEN M · 1992 to 2023
$7.3M
Structure and Function of the Acetylcholine ReceptorR37NS031744 · NINDS · MAYO CLINIC ROCHESTER · PI SINE, STEVEN M · 2001 to 2007
$4.1M
NIH HHS NS031744NIH HHS NS108874NINDS NIH HHS R01 NS031744NINDS NIH HHS R37 NS031744NINDS NIH HHS U54 NS108874
6 · The paper itself

Abstract

We describe genetic and molecular-level functional alterations in the α4β2 neuronal nicotinic acetylcholine receptor (nAChR) from a patient with sleep-related hyperkinetic epilepsy and a family history of epilepsy. Genetic sequencing revealed a heterozygous variant c.851C>G in the CHRNA4 gene encoding the α4 subunit, resulting in the missense mutation p.Ser284Trp. Patch clamp recordings from genetically engineered nAChRs incorporating the α4-Ser284Trp subunit revealed aberrant channel openings in the absence of agonist and markedly prolonged openings in its presence. Measurements of single channel current amplitude distinguished two pentameric stoichiometries of the variant nAChR containing either two or three copies of the α4-Ser284Trp subunit, each exhibiting aberrant spontaneous and prolonged agonist-elicited channel openings. The α4-Ser284 residue is highly conserved and located within the M2 transmembrane α-helix that lines the ion channel. When mapped onto the receptor’s three-dimensional structure, the larger Trp substitution sterically clashes with the M2 α-helix from the neighboring subunit, promoting expansion of the pore and stabilizing the open relative to the closed conformation of the channel. Together, the clinical, genetic, functional, and structural observations demonstrate that α4-Ser284Trp enhances channel opening, predicting increased membrane excitability and a pathogenic seizure phenotype.

Indexed as

Receptors, NicotinicCell MembraneOocytesSleepReceptors, Nicotinicgain-of-function variantion-channel conductanceion-channel gatingneuronal nicotinic acetylcholine receptorpatch-clampsingle ion-channelsleep-related hyperkinetic epilepsyspontaneous channel gating

Identifiers

PMID36292983
PMCPMC9602795
OpenAlexW4304689563

What OpenQuestion holds

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LicenceCC BY
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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.