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ATP-sensitive potassium (KATP) channels comprise four pore-forming Kir6.2 subunits and four modulatory sulfonylurea receptor (SUR) subunits. The latter belong to the ATP-binding cassette family of transporters. KATP channels are inhibited by ATP (or ADP) binding to Kir6.2 and activated by Mg-nucleotide interactions with SUR. This dual regulation enables the KATP channel to couple the metabolic state of a cell to its electrical excitability and is crucial for the KATP channel's role in regulating insulin secretion, cardiac and neuronal excitability, and vascular tone. Here, we review the regulation of the KATP channel by adenine nucleotides and present an equilibrium allosteric model for nucleotide activation and inhibition. The model can account for many experimental observations in the literature and provides testable predictions for future experiments.

Original publication

DOI

10.1016/j.bpj.2015.10.026

Type

Journal article

Journal

Biophys J

Publication Date

15/12/2015

Volume

109

Pages

2452 - 2460

Keywords

Binding Sites, Ion Channel Gating, Models, Molecular, Nucleotides, Protein Structure, Tertiary, Sulfonylurea Receptors