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@ARTICLE{Stadler:877572,
      author       = {Stadler, Andreas M. and Granzin, Joachim and Cousin,
                      Anneliese and Batra-Safferling, Renu},
      title        = {{P}hosphorylated peptide of {G} protein-coupled receptor
                      induces dimerization in activated arrestin},
      journal      = {Scientific reports},
      volume       = {10},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2020-02297},
      pages        = {10938},
      year         = {2020},
      abstract     = {Termination of the G-protein-coupled receptor signaling
                      involves phosphorylation of its C-terminus and subsequent
                      binding of the regulatory protein arrestin. In the visual
                      system, arrestin-1 preferentially binds to photoactivated
                      and phosphorylated rhodopsin and inactivates
                      phototransduction. Here, we have investigated binding of a
                      synthetic phosphopeptide of bovine rhodopsin (residues
                      323–348) to the active variants of visual arrestin-1:
                      splice variant p44, and the mutant R175E. Unlike the wild
                      type arrestin-1, both these arrestins are monomeric in
                      solution. Solution structure analysis using small angle
                      X-ray scattering supported by size exclusion chromatography
                      results reveal dimerization in both the arrestins in the
                      presence of phosphopeptide. Our results are the first
                      report, to our knowledge, on receptor-induced
                      oligomerization in arrestin, suggesting possible roles for
                      the cellular function of arrestin oligomers. Given high
                      structural homology and the similarities in their activation
                      mechanism, these results are expected to have implications
                      for all arrestin isoforms.},
      cin          = {IBI-7 / ICS-1 / JCNS-1 / IBI-8},
      ddc          = {600},
      cid          = {I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)ICS-1-20110106 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)IBI-8-20200312},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32616825},
      UT           = {WOS:000550002500046},
      doi          = {10.1038/s41598-020-67944-0},
      url          = {https://juser.fz-juelich.de/record/877572},
}