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Article

Physical and functional interaction sites in cytoplasmic domains of KCNQ1 and KCNE1 channel subunits.

American journal of physiology. Heart and circulatory physiology - 1 Feb 2020

Chen Jerri, Liu Zhenning, Creagh John, Zheng Renjian, McDonald Thomas V

Abstract excerpt

The cardiac potassium IKs current is carried by a channel complex formed from α-subunits encoded by KCNQ1 and β-subunits encoded by KCNE1. Deleterious mutations in either gene are associated with hereditary long QT syndrome. Interactions between the transmembrane domains of the α- and β-subunits determine the activation kinetics of IKs. A physical and functional interaction between COOH termini of the proteins...

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Source

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Identifiers

PMID: 31834838
DOI: 10.1152/ajpheart.00459.2019
PMCID: PMC7052629

Genes

KCNQ1

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.

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Physical and functional interaction sites in cytoplasmic domains of KCNQ1 and KCNE1 channel subunits.PMID 31834838Read ↗

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