Abstract
Voltage‐gated proton (Hv) channels have long been found with electrophysiological tools in many different cell types. However, the molecular identity of Hv channels was not discovered until 2006, when two labs independently demonstrated that the gene HVCN1 that codes for a protein called Hv1 or VSOP generates voltage‐gated proton currents when expressed in heterologous cells. Surprisingly, the sequence of Hv1/VSOP was found to be homologous to the sequence of the voltage‐sensing domain of voltage‐gated K+ channels. Recent studies have led to our present understanding of the structure of Hv1/VSOP channels and the structural underpinnings of some of the functional properties of Hv1/VSOP channels, including voltage sensing, subunit cooperativity, permeation and selectivity, pH dependence, zinc inhibition and modulation by PKC of Hv1/VSOP channels. The cloned Hv1/VSOP channels display most of the properties of native voltage‐gated proton channels. However, the molecular mechanisms underlying some of these properties are still unknown. WIREs Membr Transp Signal 2012, 1:763–777. doi: 10.1002/wmts.49
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Conflict of interest: The authors declare no conflict of interest.