Schwappach, BlancheBlancheSchwappachZerangue, NNZerangueJan, Y. N.Y. N.JanJan, L. Y.L. Y.Jan2017-09-072017-09-072000https://resolver.sub.uni-goettingen.de/purl?gro-2/2022K-ATP channels are large heteromultimeric complexes containing four subunits from the inwardly rectifying K+ channel family (Kir6.2) and four regulatory sulphonylurea receptor subunits from the ATP-binding cassette (ABC) transporter family (SUR1 and SUR2A/B). The molecular basis for interactions between these two unrelated protein families is poorly understood. Using novel trafficking-based interaction assays, coimmunoprecipitation, and current measurements, we show that the first transmembrane segment (M1) and the N terminus of Kir6.2 are involved in K-ATP assembly and gating. Additionally, the transmembrane domains, but not the nucleotide-binding domains, of SUR1 are required for interaction with Kir6.2. The identification of specific transmembrane interactions involved in K-ATP assembly may provide a clue as to how ABC proteins that transport hydrophobic substrates evolved to regulate other membrane proteins.journal_article10.1016/S0896-6273(00)81146-0107984000000867705000163144402