The first transmembrane domain (TM1) of ¦Â2-subunit binds to the transmembrane domain S1 of ¦Á-subunit in BK potassium channels
详细信息 查看全文
- 作者：Francisco J. Morera ; Abderrahmane Alioua ; Pallob Kundu ; Marcelo Salazar ; Carlos Gonzalez ; Agustin D. Martinez ; Enrico Stefani ; Ligia Toro ; Ramon Latorre
- 关键词：BK ; high-conductance voltage- and Ca2+-activated K+ channel ; TM ; transmembrane ; WB ; western blot ; Kv ; voltage-dependent potassium channels ; HEK ; human embryonic kidney cells ; Co-IP ; co-immunoprecipitation
- 刊名：FEBS Letters
- 出版年：2012
- 出版时间：30 July, 2012
- 年：2012
- 卷：586
- 期：16
- 页码：2287-2293
- 全文大小：734 K
文摘
The BK channel is one of the most broadly expressed ion channels in mammals. In many tissues, the BK channel pore-forming ¦Á-subunit is associated to an auxiliary ¦Â-subunit that modulates the voltage- and Ca2+-dependent activation of the channel. Structural components present in ¦Â-subunits that are important for the physical association with the ¦Á-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 ¦Â2-subunit are dispensable for association with the ¦Á-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 ¦Â2-subunit physically binds to the transmembrane S1 domain of the ¦Á-subunit.
Structured summary of protein interactions:
by ()