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@ARTICLE{Chaves:817747,
      author       = {Chaves, Gustavo and Derst, Christian and Franzen, Arne and
                      Mashimo, Yuta and Machida, Ryuichiro and Musset, Boris},
      title        = {{I}dentification of an {H}$_{{V}}$1 voltage-gated proton
                      channel in insects},
      journal      = {The FEBS journal},
      volume       = {283},
      number       = {8},
      issn         = {1742-464X},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2016-04390},
      pages        = {1453 - 1464},
      year         = {2016},
      abstract     = {The voltage-gated proton channel 1 (HV 1) is an important
                      component of the cellular proton extrusion machinery and is
                      essential for charge compensation during the respiratory
                      burst of phagocytes. HV 1 has been identified in a wide
                      range of eukaryotes throughout the animal kingdom, with the
                      exception of insects. Therefore, it has been proposed that
                      insects do not possess an HV 1 channel. In the present
                      study, we report the existence of an HV 1-type proton
                      channel in insects. We searched insect transcriptome shotgun
                      assembly (TSA) sequence databases and found putative HV 1
                      orthologues in various polyneopteran insects. To confirm
                      that these putative HV 1 orthologues were functional
                      channels, we studied the HV 1 channel of Nicoletia
                      phytophila (NpHV 1), an insect of the Zygentoma order, in
                      more detail. NpHV 1 comprises 239 amino acids and is $33\%$
                      identical to the human voltage-gated proton channel 1. Patch
                      clamp measurements in a heterologous expression system
                      showed proton selectivity, as well as pH- and
                      voltage-dependent gating. Interestingly, NpHV 1 shows
                      slightly enhanced pH-dependent gating compared to the human
                      channel. Mutations in the first transmembrane segment at
                      position 66 (Asp66), the presumed selectivity filter, lead
                      to a loss of proton-selective conduction, confirming the
                      importance of this aspartate residue in voltage-gated proton
                      channels.Nucleotide sequence data have been deposited in the
                      GenBank database under accession number KT780722.},
      cin          = {ICS-4},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-4-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:26866814},
      UT           = {WOS:000374680500007},
      doi          = {10.1111/febs.13680},
      url          = {https://juser.fz-juelich.de/record/817747},
}