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Article

An unconventional calmodulin-anchoring site within the AB module of Kv7.2 channels.

Journal of cell science - 15 Aug 2015

Gomis-Perez Carolina, Alaimo Alessandro, Fernandez-Orth Juncal, Alberdi Araitz, Aivar-Mateo Paloma, Bernardo-Seisdedos Ganeko, Malo Covadonga, Areso Pilar, Felipe Antonio, Villarroel Alvaro

Abstract excerpt

Calmodulin (CaM) binding to the AB module is crucial for multiple mechanisms governing the function of Kv7.2 (also known as KCNQ2) K(+) channel subunits, which mediate one of the main components of the non-inactivating K(+) M-current, a key controller of neuronal excitability. Structural analysis indicates that the CaM N-lobe engages with helix B, whereas the C-lobe anchors to the IQ site within helix A. Here, we...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 26148514
DOI: 10.1242/jcs.174128

Genes

KCNN2
KCNQ2

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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