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@ARTICLE{Chaves:910421,
      author       = {Chaves, Gustavo and Ayuyan, Artem G. and Cherny, Vladimir
                      V. and Morgan, Deri and Franzen, Arne and Fieber, Lynne and
                      Nausch, Lydia and Derst, Christian and Mahorivska, Iryna and
                      Jardin, Christophe and DeCoursey, Thomas E. and Musset,
                      Boris},
      title        = {{U}nexpected expansion of the voltage‐gated proton
                      channel family},
      journal      = {The FEBS journal},
      volume       = {290},
      number       = {4},
      issn         = {0014-2956},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2022-03810},
      pages        = {1008-1026},
      year         = {2023},
      abstract     = {Voltage-gated ion channels, whose first identified function
                      was to generate action potentials, are divided into
                      subfamilies with numerous members. The family of
                      voltage-gated proton channels (HV) is tiny. To date, all
                      species found to express HV have exclusively one gene that
                      codes for this unique ion channel. Here we report the
                      discovery and characterization of three proton channel genes
                      in the classical model system of neural plasticity, Aplysia
                      californica. The three channels (AcHV1, AcHV2, and AcHV3)
                      are distributed throughout the whole animal. Patch-clamp
                      analysis confirmed proton selectivity of these channels but
                      they all differed markedly in gating. AcHV1 gating resembled
                      HV in mammalian cells where it is responsible for proton
                      extrusion and charge compensation. AcHV2 activates more
                      negatively and conducts extensive inward proton current,
                      properties likely to acidify the cytosol. AcHV3, which
                      differs from AcHV1 and AcHV2 in lacking the first arginine
                      in the S4 helix, exhibits proton selective leak currents and
                      weak voltage dependence. We report the expansion of the
                      proton channel family, demonstrating for the first time the
                      expression of three functionally distinct proton channels in
                      a single species.},
      cin          = {IBI-1},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-1-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36062330},
      UT           = {WOS:000855393100001},
      doi          = {10.1111/febs.16617},
      url          = {https://juser.fz-juelich.de/record/910421},
}