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Article

KCNQ1 assembly and function is blocked by long-QT syndrome mutations that disrupt interaction with calmodulin.

Circulation research - 28 Apr 2006

Ghosh Smita, Nunziato Deborah A, Pitt Geoffrey S

Abstract excerpt

Calmodulin (CaM) has been recognized as an obligate subunit for many ion channels in which its function has not been clearly established. Because channel subunits associate early during channel biosynthesis, CaM may provide a mechanism for Ca(2+)-dependent regulation of channel formation. Here we show that CaM is a constitutive component of KCNQ1 K+ channels, the most commonly mutated long-QT syndrome (LQTS)...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 16556866
DOI: 10.1161/01.RES.0000218863.44140.f2

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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KCNQ1 assembly and function is blocked by long-QT syndrome mutations that disrupt interaction with calmodulin.PMID 16556866Read ↗

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