Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

An epilepsy-associated KV1.2 charge-transfer-center mutation impairs KV1.2 and KV1.4 trafficking.

Proceedings of the National Academy of Sciences of the United States of America - 26 Apr 2022

Nilsson Michelle, Lindström Sarah H, Kaneko Maki, Wang Kaiqian, Minguez-Viñas Teresa, Angelini Marina, Steccanella Federica, Holder Deborah, Ottolia Michela, Olcese Riccardo, Pantazis Antonios

Abstract excerpt

We report on a heterozygous KCNA2 variant in a child with epilepsy. KCNA2 encodes KV1.2 subunits, which form homotetrameric potassium channels and participate in heterotetrameric channel complexes with other KV1-family subunits, regulating neuronal excitability. The mutation causes substitution F233S at the KV1.2 charge transfer center of the voltage-sensing domain. Immunocytochemical trafficking assays showed...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Membrane
Share to Child

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Epilepsy

Share to Kv1.1 Potassium Channel

Share to Mutation

Share to Potassium

Share to Potassium Channels

Source

Open in PubMed Open full text

Identifiers

PMID: 35439054
DOI: 10.1073/pnas.2113675119
PMCID: PMC9169947

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An epilepsy-associated KV1.2 charge-transfer-center mutation impairs KV1.2 and KV1.4 trafficking.PMID 35439054Read ↗

Two epilepsy-associated variants in KCNA2 (KV 1.2) at position H310 oppositely affect channel functional expression.Semantic proximity Read ↗

Tracking the motion of the KV1.2 voltage sensor reveals the molecular perturbations caused by a de novo mutation in a case of epilepsy.Semantic proximity Read ↗

High-throughput discovery of trafficking-deficient variants in the cardiac potassium channel KV11.1.Semantic proximity Read ↗

Molecular pathogenesis of long QT syndrome type 2Semantic proximity Read ↗

High throughput Characterization of <i>KCNB1</i> variants Associated with Developmental and Epileptic EncephalopathySemantic proximity Read ↗

Biophysical and structural mechanisms of epilepsy-associated mutations in the S4-S5 Linker of KCNQ2 channels.Semantic proximity Read ↗

Plural molecular and cellular mechanisms of pore domain <i>KCNQ2</i> encephalopathySemantic proximity Read ↗

Inwardly Rectifying Potassium Channel Kir2.1 and its “Kir-ious” Regulation by Protein Trafficking and Roles in Development and DiseaseSemantic proximity Read ↗

C-terminal domain of Kv4.2 and associated KChIP2 interactions regulate functional expression and gating of Kv4.2.Semantic proximity Read ↗

High-throughput discovery of trafficking-deficient variants in the cardiac potassium channel <i>KCNH2</i> : Deep mutational scan of <i>KCNH2</i> traffickingSemantic proximity Read ↗

Type I TARPs regulate Kv7.2 potassium channels and susceptibility to seizuresSemantic proximity Read ↗

A novel epileptic encephalopathy mutation in <i>KCNB1</i> disrupts Kv2.1 ion selectivity, expression, and localizationSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.