Molecular basis for K(ATP) assembly: transmembrane interactions mediate association of a K+ channel with an ABC transporter

Neuron. 2000 Apr;26(1):155-67. doi: 10.1016/s0896-6273(00)81146-0.


K(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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • ATP Binding Cassette Transporter 1
  • ATP-Binding Cassette Transporters / chemistry
  • ATP-Binding Cassette Transporters / metabolism*
  • Animals
  • Glycoproteins / chemistry
  • Glycoproteins / metabolism*
  • Humans
  • Membrane Potentials / physiology
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Potassium Channels / chemistry
  • Potassium Channels / metabolism*
  • Xenopus


  • ATP Binding Cassette Transporter 1
  • ATP-Binding Cassette Transporters
  • Glycoproteins
  • Membrane Proteins
  • Potassium Channels