Ontology highlight
ABSTRACT:
SUBMITTER: Qiu F
PROVIDER: S-EPMC3558936 | biostudies-literature | 2013 Jan
REPOSITORIES: biostudies-literature
Qiu Feng F Rebolledo Santiago S Gonzalez Carlos C Larsson H Peter HP
Neuron 20130101 2
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 properti ...[more]