Subunit interactions during cooperative opening of voltage-gated proton channels.
Subunit interactions during cooperative opening of voltage-gated proton channels.
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DOI:
10.1016/j.neuron.2012.12.021
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发表时间:
2013-01-23
期刊:
影响因子:
16.2
通讯作者:
Larsson HP
中科院分区:
文献类型:
--
作者:
Qiu F;Rebolledo S;Gonzalez C;Larsson HP
Voltage-gated proton (Hv1) channels are dimers, where each subunit has a separate permeation pathway. However, opening of the two pathways is highly cooperative. It is unclear how Hv1 channels open their permeation pathways, because Hv1 channels lack a classic pore domain. Using voltage clamp fluorometry, we here detect two conformational changes reported by a fluorophore attached to the voltage sensor S4 in Hv1 channels. The first is voltage dependent and precedes channel opening, with properties consistent with reporting on independent S4 charge movements in the two subunits. The second is less voltage dependent and closely correlates with channel opening. Mutations that reduce dimerization or alter the intersubunit interface affect both the second conformational change and channel opening. These observations suggest that, following an initial S4 charge movement in the two subunits, there is a second, cooperative conformational change, involving interactions between subunits, that opens both pathways in Hv1 channels.
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影响因子:
25
作者:
通讯作者:
--
DOI:
10.1085/jgp.200910379
发表时间:
2010-07
期刊:
The Journal of general physiology
影响因子:
--
作者:
Iovannisci D;Illek B;Fischer H
通讯作者:
Fischer H
影响因子:
16.8
作者:
通讯作者:
--
DOI:
10.1085/jgp.103.2.279
发表时间:
1994-02
期刊:
The Journal of general physiology
影响因子:
--
作者:
Zagotta WN;Hoshi T;Dittman J;Aldrich RW
通讯作者:
Aldrich RW
影响因子:
16.2
作者:
Hong L;Pathak MM;Kim IH;Ta D;Tombola F
通讯作者:
Tombola F