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• W2015957314 abstract "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." @default.
• W2015957314 created "2016-06-24" @default.
• W2015957314 creator A5013957351 @default.
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• W2015957314 creator A5080674124 @default.
• W2015957314 creator A5086117298 @default.
• W2015957314 date "2013-01-01" @default.
• W2015957314 modified "2023-10-18" @default.
• W2015957314 title "Subunit Interactions during Cooperative Opening of Voltage-Gated Proton Channels" @default.
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• W2015957314 doi "https://doi.org/10.1016/j.neuron.2012.12.021" @default.
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