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@ARTICLE{Govorunova:943338,
      author       = {Govorunova, Elena G. and Sineshchekov, Oleg A. and Brown,
                      Leonid S. and Bondar, Ana-Nicoleta and Spudich, John L.},
      title        = {{S}tructural {F}oundations of {P}otassium {S}electivity in
                      {C}hannelrhodopsins},
      journal      = {mBio},
      volume       = {13},
      number       = {6},
      issn         = {2161-2129},
      address      = {Washington, DC},
      publisher    = {American Society for Microbiology},
      reportid     = {FZJ-2023-00944},
      pages        = {e03039-22},
      year         = {2022},
      abstract     = {Potassium-selective channelrhodopsins (KCRs) are
                      light-gated K+ channels recently found in the stramenopile
                      protist Hyphochytrium catenoides. When expressed in neurons,
                      KCRs enable high-precision optical inhibition of spiking
                      (optogenetic silencing). KCRs are capable of discriminating
                      K+ from Na+ without the conventional K+ selectivity filter
                      found in classical K+ channels. The genome of H. catenoides
                      also encodes a third paralog that is more permeable for Na+
                      than for K+. To identify structural motifs responsible for
                      the unusual K+ selectivity of KCRs, we systematically
                      analyzed a series of chimeras and mutants of this protein.
                      We found that mutations of three critical residues in the
                      paralog convert its Na+-selective channel into a
                      K+-selective one. Our characterization of homologous
                      proteins from other protists (Colponema vietnamica,
                      Cafeteria burkhardae, and Chromera velia) and metagenomic
                      samples confirmed the importance of these residues for K+
                      selectivity. We also show that Trp102 and Asp116, conserved
                      in all three H. catenoides paralogs, are necessary, although
                      not sufficient, for K+ selectivity. Our results provide the
                      foundation for further engineering of KCRs for optogenetic
                      needs.},
      cin          = {IAS-5 / INM-9},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36413022},
      UT           = {WOS:000890586800001},
      doi          = {10.1128/mbio.03039-22},
      url          = {https://juser.fz-juelich.de/record/943338},
}