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@ARTICLE{Bestsennaia:1023075,
      author       = {Bestsennaia, Ekaterina and Maslov, Ivan and Balandin, Taras
                      and Alekseev, Alexey and Yudenko, Anna and Abu Shamseye,
                      Assalla and Zabelskii, Dmitrii and Baumann, Arnd and
                      Catapano, Claudia and Karathanasis, Christos and Gordeliy,
                      Valentin and Heilemann, Mike and Gensch, Thomas and
                      Borshchevskiy, Valentin},
      title        = {{C}hannelrhodopsin‐2 {O}ligomerization in {C}ell
                      {M}embrane {R}evealed by {P}hoto‐{A}ctivated
                      {L}ocalization {M}icroscopy},
      journal      = {Angewandte Chemie},
      volume       = {63},
      number       = {11},
      issn         = {1433-7851},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {FZJ-2024-01648},
      pages        = {e202307555},
      year         = {2024},
      abstract     = {Microbialrhodopsinsare retinalmembraneproteinsthat founda
                      broadapplicationin optogenetics.Theoligomericstate of
                      rhodopsinsis importantfor their functionalityand
                      stability.Of particularinterestis the oligomericstate in the
                      cellularnativemembraneenvironment.Fluorescencemicroscopyprovidespowerfultools
                      to determinetheoligomericstate of membraneproteinsdirectlyin
                      cells. Amongthese methodsis
                      quantitativephotoactivatedlocalizationmicroscopy(qPALM)allowingthe
                      investigationof molecularorganizationat the level of
                      singleproteinclusters.Here,we applyqPALMto investigatethe
                      oligomericstate of the first and most used optogenetictool
                      Channelrhodopsin-2(ChR2)in the plasmamembraneof
                      eukaryoticcells. ChR2appearedpredominantlyas a dimerin the
                      cell membraneanddid not form higheroligomers.The
                      disulfidebondsbetweenCys34and Cys36of
                      adjacentChR2monomerswere notrequiredfor dimerformationand
                      mutationsdisruptingthese bondsresultedin only
                      partialmonomerizationof ChR2.The
                      monomericfractionincreasedwhenthe total concentrationof
                      mutantChR2in the membranewas low. Thedissociationconstantwas
                      estimatedfor this partiallymonomerizedmutantChR2as 2.2�0.9
                      proteins/μm2. Our findingsare importantfor understandingthe
                      mechanisticbasis of ChR2activityas well as for
                      improvingexistingand developingfutureoptogenetictools.},
      cin          = {IBI-1 / IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-1-20200312 / I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {38226794},
      UT           = {WOS:001155410200001},
      doi          = {10.1002/anie.202307555},
      url          = {https://juser.fz-juelich.de/record/1023075},
}