Insights into the structure and function of HV1 from a meta-analysis of mutation studies

被引:30
作者
DeCoursey, Thomas E. [1 ]
Morgan, Deri [1 ]
Musset, Boris [2 ]
Cherny, Vladimir V. [1 ]
机构
[1] Rush Univ, Dept Mol Biophys & Physiol, Chicago, IL 60612 USA
[2] PMU Klinikum Nurnberg, Inst Physiol, D-90419 Nurnberg, Germany
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
GATED PROTON CHANNEL; HYDROGEN-ION CURRENTS; ALVEOLAR EPITHELIAL-CELLS; OXIDASE-RELATED PROTON; F1F0 ATP SYNTHASE; NADPH-OXIDASE; H+ CHANNEL; HUMAN-NEUTROPHILS; VOLTAGE-SENSOR; ELECTRON CURRENTS;
D O I
10.1085/jgp.201611619
中图分类号
Q4 [生理学];
学科分类号
071003 ;
摘要
The voltage-gated proton channel (H(V)1) is a widely distributed, proton-specific ion channel with unique properties. Since 2006, when genes for H(V)1 were identified, a vast array of mutations have been generated and characterized. Accessing this potentially useful resource is hindered, however, by the sheer number of mutations and interspecies differences in amino acid numbering. This review organizes all existing information in a logical manner to allow swift identification of studies that have characterized any particular mutation. Although much can be gained from this meta-analysis, important questions about the inner workings of H(V)1 await future revelation.
引用
收藏
页码:97 / 118
页数:22
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