Abstract:
: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.
journal_name
Neuronjournal_title
Neuronauthors
Schwappach B,Zerangue N,Jan YN,Jan LYdoi
10.1016/s0896-6273(00)81146-0subject
Has Abstractpub_date
2000-04-01 00:00:00pages
155-67issue
1eissn
0896-6273issn
1097-4199pii
S0896-6273(00)81146-0journal_volume
26pub_type
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