Control of Hv1 Voltage-Gated Proton Channel Opening by Changes in the Transmembrane Voltage and pH Gradients

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Selectivity Mechanism of the Voltage-gated Proton Channel, HV1

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The Voltage-Gated Proton Channel Hv1 Has Two Pores, Each Controlled by One Voltage Sensor

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Voltage-Sensing Domain of Voltage-Gated Proton Channel Hv1 Shares Mechanism of Block with Pore Domains

Voltage-gated sodium, potassium, and calcium channels are made of a pore domain (PD) controlled by four voltage-sensing domains (VSDs). The PD contains the ion permeation pathway and the activation gate located on the intracellular side of the membrane. A large number of small molecules are known to inhibit the PD by acting as open channel blockers. The voltage-gated proton channel Hv1 is made ...

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Hv1 proton channel opening is preceded by a voltage-independent transition.

The voltage sensing domain (VSD) of the voltage-gated proton channel Hv1 mediates a H(+)-selective conductance that is coordinately controlled by the membrane potential (V) and the transmembrane pH gradient (ΔpH). Allosteric control of Hv1 channel opening by ΔpH (V-ΔpH coupling) is manifested by a characteristic shift of approximately 40 mV per ΔpH unit in the activation. To further understand ...

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ژورنال

عنوان ژورنال: Biophysical Journal

سال: 2012

ISSN: 0006-3495

DOI: 10.1016/j.bpj.2011.11.225