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@ARTICLE{Gunkel:137875,
      author       = {Gunkel, Monika and Schöneberg, Johannes and Alkhaldi,
                      Weaam and Irsen, Stephan and Noé, Frank and Kaupp, U
                      Benjamin and Alamoudi, Ashraf},
      title        = {{H}igher-order architecture of rhodopsin in intact
                      photoreceptors and its implication for phototransduction
                      kinetics.},
      journal      = {Structure},
      volume       = {23},
      number       = {4},
      issn         = {0969-2126},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {DZNE-2020-04197},
      pages        = {628-638},
      year         = {2015},
      abstract     = {The visual pigment rhodopsin belongs to the family of G
                      protein-coupled receptors that can form higher oligomers. It
                      is controversial whether rhodopsin forms oligomers and
                      whether oligomers are functionally relevant. Here, we study
                      rhodopsin organization in cryosections of dark-adapted mouse
                      rod photoreceptors by cryoelectron tomography. We identify
                      four hierarchical levels of organization. Rhodopsin forms
                      dimers; at least ten dimers form a row. Rows form pairs
                      (tracks) that are aligned parallel to the disk incisures.
                      Particle-based simulation shows that the combination of
                      tracks with fast precomplex formation, i.e. rapid
                      association and dissociation between inactive rhodopsin and
                      the G protein transducin, leads to kinetic trapping:
                      rhodopsin first activates transducin from its own track,
                      whereas recruitment of transducin from other tracks proceeds
                      more slowly. The trap mechanism could produce uniform
                      single-photon responses independent of rhodopsin lifetime.
                      In general, tracks might provide a platform that coordinates
                      the spatiotemporal interaction of signaling molecules.},
      keywords     = {Animals / Kinetics / Mice / Mice, Inbred C57BL /
                      Photoreceptor Cells: metabolism / Photoreceptor Cells:
                      ultrastructure / Protein Binding / Protein Multimerization /
                      Rhodopsin: chemistry / Rhodopsin: metabolism / Transducin:
                      metabolism / Vision, Ocular / Rhodopsin (NLM Chemicals) /
                      Transducin (NLM Chemicals)},
      cin          = {AG Alamoudi},
      ddc          = {540},
      cid          = {I:(DE-2719)1013012},
      pnm          = {341 - Molecular Signaling (POF3-341)},
      pid          = {G:(DE-HGF)POF3-341},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:25728926},
      doi          = {10.1016/j.str.2015.01.015},
      url          = {https://pub.dzne.de/record/137875},
}