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

Journal article

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 novel channels are also inhibited by intracellular pH within the physiological r...

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Authors: Casamassima, M; D'Adamo, M; Pessia, M; Tucker, S

• Publication status: Published
• Journal: Journal of biological chemistry
• Volume: 278
• Issue: 44
• Pages: 43533-43540
• Publication date: 2003-10-01
• DOI: 10.1074/jbc.m306596200
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Protein Binding; Time Factors; Xenopus laevis; Models, Molecular; Potassium; Amino Acid Sequence; Cloning, Molecular; Mutation; Protein Structure, Tertiary; Potassium Channels, Inwardly Rectifying; Electrophysiology; Animals; Hydrogen-Ion Concentration; Cytoplasm; Sequence Homology, Amino Acid; Hydrogen; Molecular Sequence Data