The first transmembrane domain (TM1) of ß2-subunit binds to the transmembrane domain S1 of α-subunit in BK potassium channels.
FEBS Lett
; 586(16): 2287-93, 2012 Jul 30.
Article
em En
| MEDLINE
| ID: mdl-22710124
ABSTRACT
The BK channel is one of the most broadly expressed ion channels in mammals. In many tissues, the BK channel pore-forming α-subunit is associated to an auxiliary ß-subunit that modulates the voltage- and Ca(2+)-dependent activation of the channel. Structural components present in ß-subunits that are important for the physical association with the α-subunit are yet unknown. Here, we show through co-immunoprecipitation that the intracellular C-terminus, the second transmembrane domain (TM2) and the extracellular loop of the ß2-subunit are dispensable for association with the α-subunit pointing transmembrane domain 1 (TM1) as responsible for the interaction. Indeed, the TOXCAT assay for transmembrane protein-protein interactions demonstrated for the first time that TM1 of the ß2-subunit physically binds to the transmembrane S1 domain of the α-subunit.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article