期刊
FEBS LETTERS
卷 586, 期 16, 页码 2287-2293出版社
WILEY
DOI: 10.1016/j.febslet.2012.05.066
关键词
BK channels; beta 2-Subunit; TOXCAT assay; Transmembrane domain TM1; BK alpha and beta-subunits interactions
资金
- FONDECYT [1110430, 1090573, 1120802, S-2012-13]
- National Institutes of Health [HL088640, HL54970, HL096740]
- CONICYT
- Beca de Estadia en Centros Internacionales de Investigacion Cientifica, Direccion de Postgrado UACH
- Minesterio de Economia, Fomento y Turismo
The BK channel is one of the most broadly expressed ion channels in mammals. In many tissues, the BK channel pore-forming alpha-subunit is associated to an auxiliary beta-subunit that modulates the voltage- and Ca2+-dependent activation of the channel. Structural components present in beta-subunits that are important for the physical association with the alpha-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 beta 2-subunit are dispensable for association with the alpha-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 beta 2-subunit physically binds to the transmembrane S1 domain of the alpha-subunit.
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