The RCK1 domain of the human BKCa channel transduces Ca2+ binding into structural rearrangements.
The RCK1 domain of the human BKCa channel transduces Ca2+ binding into structural rearrangements.
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DOI：
10.1085/jgp.200910374
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发表时间：
2010-08
期刊：
影响因子：
--
通讯作者：
Olcese R
中科院分区：
文献类型：
--
作者：
Yusifov T;Javaherian AD;Pantazis A;Gandhi CS;Olcese R
Large-conductance voltage- and Ca2+-activated K+ (BKCa) channels play a fundamental role in cellular function by integrating information from their voltage and Ca2+ sensors to control membrane potential and Ca2+ homeostasis. The molecular mechanism of Ca2+-dependent regulation of BKCa channels is unknown, but likely relies on the operation of two cytosolic domains, regulator of K+ conductance (RCK)1 and RCK2. Using solution-based investigations, we demonstrate that the purified BKCa RCK1 domain adopts an α/β fold, binds Ca2+, and assembles into an octameric superstructure similar to prokaryotic RCK domains. Results from steady-state and time-resolved spectroscopy reveal Ca2+-induced conformational changes in physiologically relevant [Ca2+]. The neutralization of residues known to be involved in high-affinity Ca2+ sensing (D362 and D367) prevented Ca2+-induced structural transitions in RCK1 but did not abolish Ca2+ binding. We provide evidence that the RCK1 domain is a high-affinity Ca2+ sensor that transduces Ca2+ binding into structural rearrangements, likely representing elementary steps in the Ca2+-dependent activation of human BKCa channels.
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DOI：
10.1085/jgp.200509419
发表时间：
2006-06
期刊：
The Journal of general physiology
影响因子：
--
作者：
Fodor AA;Aldrich RW
通讯作者：
Aldrich RW
影响因子：
3.4
作者：
Kim, Hyun-Ju;Lim, Hyun-Ho;Park, Chul-Seung
通讯作者：
Park, Chul-Seung
影响因子：
16
作者：
Hilge, M;Aelen, J;Vuister, GW
通讯作者：
Vuister, GW
影响因子：
16.8
作者：
Hou, Shangwei;Xu, Rong;Hoshi, Toshinori
通讯作者：
Hoshi, Toshinori
DOI：
10.1073/pnas.0800304105
发表时间：
2008-03-11
影响因子：
11.1
作者：
Hou, Shangwei;Xu, Rong;Hoshi, Toshinori
通讯作者：
Hoshi, Toshinori