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@ARTICLE{CruzGarcia:905991,
      author       = {Cruz-Garcia, Yiliam and Barkovits, Katalin and Kohlhaas,
                      Michael and Pickel, Simone and Gulentz, Michelle and Heindl,
                      Cornelia and Pfeiffer, Kathy and Eder-Negrin, Petra and
                      Maack, Christoph and Marcus, Katrin and Kuhn, Michaela and
                      Miranda Laferte, Erick},
      title        = {{N}anoenviroments of the β-{S}ubunit of {L}-{T}ype
                      {V}oltage-{G}ated {C}alcium {C}hannels in {A}dult
                      {C}ardiomyocytes},
      journal      = {Frontiers in cell and developmental biology},
      volume       = {9},
      issn         = {2296-634X},
      address      = {Lausanne},
      publisher    = {Frontiers Media},
      reportid     = {FZJ-2022-01165},
      pages        = {724778},
      year         = {2022},
      abstract     = {In cardiomyocytes, Ca2+ influx through L-type voltage-gated
                      calcium channels (LTCCs) following membrane depolarization
                      regulates crucial Ca2+-dependent processes including
                      duration and amplitude of the action potentials and
                      excitation-contraction coupling. LTCCs are heteromultimeric
                      proteins composed of the Cavα1, Cavβ, Cavα2δ and Cavγ
                      subunits. Here, using ascorbate peroxidase (APEX2)-mediated
                      proximity labeling and quantitative proteomics, we
                      identified 61 proteins in the nanoenvironments of Cavβ2 in
                      cardiomyocytes. These proteins are involved in diverse
                      cellular functions such as cellular trafficking, cardiac
                      contraction, sarcomere organization and
                      excitation-contraction coupling. Moreover, pull-down assays
                      and co-immunoprecipitation analyses revealed that Cavβ2
                      interacts with the ryanodine receptor 2 (RyR2) in adult
                      cardiomyocytes, probably coupling LTCCs and the RyR2 into a
                      supramolecular complex at the dyads. This interaction is
                      mediated by the Src-homology 3 domain of Cavβ2 and is
                      necessary for an effective pacing frequency-dependent
                      increase of the Ca2+-induced Ca2+ release mechanism in
                      cardiomyocytes.},
      cin          = {IBI-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-1-20200312},
      pnm          = {5243 - Information Processing in Distributed Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5243},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35047492},
      UT           = {WOS:000751080600001},
      doi          = {10.3389/fcell.2021.724778},
      url          = {https://juser.fz-juelich.de/record/905991},
}