Identification of a heteromeric interaction that influences the rectification, gating, and pH sensitivity of Kir4.1/Kir5.1 potassium channels.

doi:10.1074/jbc.M306596200

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Article

Identification of a heteromeric interaction that influences the rectification, gating, and pH sensitivity of Kir4.1/Kir5.1 potassium channels.

The Journal of biological chemistry - 31 Oct 2003

Casamassima Maria, D'Adamo M Cristina, Pessia Mauro, Tucker Stephen J

Abstract excerpt

Heteromultimerization between different potassium channel subunits can generate channels with novel functional properties and thus contributes to the rich functional diversity of this gene family. The inwardly rectifying potassium channel subunit Kir5.1 exhibits highly selective heteromultimerization with Kir4.1 to generate heteromeric Kir4.1/Kir5.1 channels with unique rectification and kinetic properties. These...

Topics

Amino Acid Sequence
Animals
Cloning, Molecular
Cytoplasm
Electrophysiology
Hydrogen
Hydrogen-Ion Concentration
Models, Molecular
Molecular Sequence Data
Mutation
Potassium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Potassium Channels, Inwardly Rectifying

Protein Binding

Protein Structure, Tertiary

Sequence Homology, Amino Acid

Time Factors

Xenopus laevis

Source

Open in PubMed

Identifiers

PMID: 12923169
DOI: 10.1074/jbc.M306596200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-12923169-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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