Molecular structure and function of Hv1 channels

Santiago Rebolledo, Feng Qiu, H. Peter Larsson

Research output: Contribution to journalReview articlepeer-review

4 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)763-777
Number of pages15
JournalWiley Interdisciplinary Reviews: Membrane Transport and Signaling
Issue number6
StatePublished - Nov 1 2012

ASJC Scopus subject areas

  • Biophysics
  • Cellular and Molecular Neuroscience


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