Architecture and gating of Hv1 proton channels

被引:18
|
作者
Tombola, Francesco [2 ]
Ulbrich, Maximilian H.
Isacoff, Ehud Y. [1 ,3 ,4 ]
机构
[1] Univ Calif Berkeley, MCB, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
[2] Univ Calif Irvine, Dept Physiol & Biophys, Irvine, CA 92697 USA
[3] Univ Calif Berkeley, Lawrence Berkeley Lab, Div Mat Sci, Berkeley, CA 94720 USA
[4] Univ Calif Berkeley, Lawrence Berkeley Lab, Phys Biosci Div, Berkeley, CA 94720 USA
来源
JOURNAL OF PHYSIOLOGY-LONDON | 2009年 / 587卷 / 22期
基金
美国国家卫生研究院;
关键词
SHAKER K+ CHANNEL; VOLTAGE SENSOR; CHLORIDE CHANNEL; SODIUM-CHANNELS; MOLECULAR-BASIS; ION-PERMEATION; PORE; CURRENTS; DOMAIN; REVEALS;
D O I
10.1113/jphysiol.2009.180265
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Voltage-gated proton channels have been described in different cells and organisms since the early '80s, but the first member of the family, Hv1, was cloned only recently. The Hv1 channel was found to contain a voltage-sensing domain (VSD), similar to those of voltage-gated sodium, potassium and calcium channels. All these other channels also contain a pore domain, which forms a central pore at the interface of the four subunits. The pore domain is missing in Hv1. This raised several questions on the location of the proton pore and on the mechanism of gating. Here, we briefly review our effort to understand the structural organization of Hv1 channels and discuss the relationship between the gating of Hv1 and the gating of ion-conducting pores recently discovered in the VSDs of mutant voltage-gated potassium and sodium channels.
引用
收藏
页码:5325 / 5329
页数:5
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