Structural highlights
Function
[HVCN1_HUMAN] Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis.[1] [2] [3]
Publication Abstract from PubMed
The voltage-gated proton channel Hv1 has a voltage sensor domain but lacks a pore domain. Although the C-terminal domain of Hv1 is known to be responsible for dimeric architecture of the channel, its role and structure are not known. We report that the full-length Hv1 is mainly localized in intracellular compartment membranes rather than the plasma membrane. Truncation of either the N or C terminus alone or both together revealed that the N-terminal deletion did not alter localization, but deletion of the C terminus either alone or together with the N terminus resulted in expression throughout the cell. These results indicate that the C terminus is essential for Hv1 localization but not the N terminus. In the 2.0 A structure of the C-terminal domain, the two monomers form a dimer via a parallel alpha-helical coiled-coil, in which one chloride ion binds with the Neta atom of Arg(264). A pH-dependent structural change of the protein has been observed, but it remains a dimer irrespective of pH value.
The role and structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1.,Li SJ, Zhao Q, Zhou Q, Unno H, Zhai Y, Sun F J Biol Chem. 2010 Apr 16;285(16):12047-54. Epub 2010 Feb 10. PMID:20147290[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ramsey IS, Moran MM, Chong JA, Clapham DE. A voltage-gated proton-selective channel lacking the pore domain. Nature. 2006 Apr 27;440(7088):1213-6. Epub 2006 Mar 22. PMID:16554753 doi:http://dx.doi.org/nature04700
- ↑ Musset B, Capasso M, Cherny VV, Morgan D, Bhamrah M, Dyer MJ, DeCoursey TE. Identification of Thr29 as a critical phosphorylation site that activates the human proton channel Hvcn1 in leukocytes. J Biol Chem. 2010 Feb 19;285(8):5117-21. doi: 10.1074/jbc.C109.082727. Epub 2009 , Dec 26. PMID:20037153 doi:http://dx.doi.org/10.1074/jbc.C109.082727
- ↑ Musset B, Smith SM, Rajan S, Morgan D, Cherny VV, Decoursey TE. Aspartate 112 is the selectivity filter of the human voltage-gated proton channel. Nature. 2011 Oct 23;480(7376):273-7. doi: 10.1038/nature10557. PMID:22020278 doi:http://dx.doi.org/10.1038/nature10557
- ↑ Li SJ, Zhao Q, Zhou Q, Unno H, Zhai Y, Sun F. The role and structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1. J Biol Chem. 2010 Apr 16;285(16):12047-54. Epub 2010 Feb 10. PMID:20147290 doi:10.1074/jbc.M109.040360
