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HVCN1

Protein-coding gene in the species Homo sapiens

Protein-coding gene in the species Homo sapiens

Voltage-gated hydrogen channel 1 is a protein that in humans is encoded by the HVCN1 gene.

Voltage-gated hydrogen channel 1 is a voltage-gated proton channel that has been shown to allow proton transport into phagosomes and out of many types of cells including spermatozoa, electrically excitable cells and respiratory epithelial cells. The proton-conducting HVCN1 channel has only transmembrane domains corresponding to the S1-S4 voltage sensing domains (VSD) of voltage-gated potassium channels and voltage-gated sodium channels. Molecular simulation is consistent with a water-filled pore that can function as a "water wire" for allowing hydrogen bonded H+ to cross the membrane. However, mutation of Asp112 in human Hv1 results in anion permeation, suggesting that obligatory protonation of Asp produces proton selectivity. Quantum mechanical calculations show that the Asp-Arg interaction can produce proton selective permeation. The HVCN1 protein has been shown to exist as a dimer with two functioning pores. Like other VSD channels, HVCN1 channels conduct ions about 1000-fold slower than channels formed by tetrameric S5-S6 central pores.

As a drug target

Small molecule inhibitors of the HVCN1 channel are being developed as chemotherapeutics and anti-inflammatory agents.

References

References

  1. (August 2006). "Charge compensation during the phagocyte respiratory burst". Biochimica et Biophysica Acta (BBA) - Bioenergetics.
  2. (March 2010). "HVCN1 modulates BCR signal strength via regulation of BCR-dependent generation of reactive oxygen species". Nature Immunology.
  3. (January 2011). "pH regulation and beyond: unanticipated functions for the voltage-gated proton channel, HVCN1". Trends in Cell Biology.
  4. (April 2009). "Functional reconstitution of purified human Hv1 H+ channels". Journal of Molecular Biology.
  5. (February 2012). "Water wires in atomistic models of the Hv1 proton channel". Biochimica et Biophysica Acta (BBA) - Biomembranes.
  6. (July 2010). "An aqueous H+ permeation pathway in the voltage-gated proton channel Hv1". Nature Structural & Molecular Biology.
  7. (23 October 2011). "Aspartate 112 is the selectivity filter of the human voltage-gated proton channel.". Nature.
  8. (8 May 2015). "Selectivity Mechanism of the Voltage-gated Proton Channel, HV1.". Scientific Reports.
  9. (January 2010). "Strong cooperativity between subunits in voltage-gated proton channels". Nature Structural & Molecular Biology.
  10. (January 2010). "The opening of the two pores of the Hv1 voltage-gated proton channel is tuned by cooperativity". Nature Structural & Molecular Biology.
  11. (November 2008). "Voltage-gated proton channels: what's next?". The Journal of Physiology.
  12. (January 2013). "Voltage-sensing domain of voltage-gated proton channel Hv1 shares mechanism of block with pore domains". Neuron.
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