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@ARTICLE{Grauel:138809,
      author       = {Grauel, M Katharina and Maglione, Marta and Reddy-Alla,
                      Suneel and Willmes, Claudia G and Brockmann, Marisa M and
                      Trimbuch, Thorsten and Rosenmund, Tanja and Pangalos, Maria
                      and Vardar, Gülçin and Stumpf, Alexander and Walter,
                      Alexander M and Rost, Benjamin R and Eickholt, Britta J and
                      Haucke, Volker and Schmitz, Dietmar and Sigrist, Stephan J
                      and Rosenmund, Christian},
      title        = {{RIM}-binding protein 2 regulates release probability by
                      fine-tuning calcium channel localization at murine
                      hippocampal synapses.},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {113},
      number       = {41},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {DZNE-2020-05131},
      pages        = {11615-11620},
      year         = {2016},
      abstract     = {The tight spatial coupling of synaptic vesicles and
                      voltage-gated Ca2+ channels (CaVs) ensures efficient action
                      potential-triggered neurotransmitter release from
                      presynaptic active zones (AZs). Rab-interacting
                      molecule-binding proteins (RIM-BPs) interact with Ca2+
                      channels and via RIM with other components of the release
                      machinery. Although human RIM-BPs have been implicated in
                      autism spectrum disorders, little is known about the role of
                      mammalian RIM-BPs in synaptic transmission. We investigated
                      RIM-BP2-deficient murine hippocampal neurons in cultures and
                      slices. Short-term facilitation is significantly enhanced in
                      both model systems. Detailed analysis in culture revealed a
                      reduction in initial release probability, which presumably
                      underlies the increased short-term facilitation.
                      Superresolution microscopy revealed an impairment in CaV2.1
                      clustering at AZs, which likely alters Ca2+ nanodomains at
                      release sites and thereby affects release probability.
                      Additional deletion of RIM-BP1 does not exacerbate the
                      phenotype, indicating that RIM-BP2 is the dominating RIM-BP
                      isoform at these synapses.},
      keywords     = {Action Potentials / Animals / Calcium: metabolism / Calcium
                      Channels: metabolism / Cells, Cultured /
                      Electrophysiological Phenomena / Female / Gene Deletion /
                      Gene Expression / Gene Targeting / Genetic Loci /
                      Hippocampus: metabolism / Male / Mice / Mice, Knockout /
                      Neurons: metabolism / Phenotype / Protein Transport /
                      Synapses: metabolism / Synaptic Transmission: genetics /
                      Synaptic Vesicles: metabolism / Calcium Channels (NLM
                      Chemicals) / Calcium (NLM Chemicals)},
      cin          = {AG Schmitz 1},
      ddc          = {500},
      cid          = {I:(DE-2719)1810004},
      pnm          = {341 - Molecular Signaling (POF3-341)},
      pid          = {G:(DE-HGF)POF3-341},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27671655},
      pmc          = {pmc:PMC5068320},
      doi          = {10.1073/pnas.1605256113},
      url          = {https://pub.dzne.de/record/138809},
}