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@ARTICLE{Kroon:281370,
      author       = {Kroon, Cristina and Bareesel, Shannon and Perez, Gerard
                      Aguilar and Nagy-Herczeg, Domonkos and Ranti, Dimitra and
                      Syropoulou, Vasiliki and Coveney, Sandra and Kirchner,
                      Marieluise and Gimber, Niclas and Bintig, Willem and Brosig,
                      Annika and Braune, Georg and Textoris-Taube, Kathrin and
                      Zolnik, Timothy A. and Mertins, Philipp and Schmoranzer, Jan
                      and Milovanovic, Dragomir and Leondaritis, George and
                      Eickholt, Britta J.},
      title        = {{P}hosphorylation of presynaptic {PLPPR}3 controls synaptic
                      vesicle release},
      journal      = {iScience},
      volume       = {28},
      number       = {9},
      issn         = {2589-0042},
      address      = {St. Louis},
      publisher    = {Elsevier},
      reportid     = {DZNE-2025-01117},
      pages        = {113435},
      year         = {2025},
      abstract     = {Phospholipid-phosphatase-related protein 3 (PLPPR3) belongs
                      to a family of transmembrane proteins highly expressed in
                      the nervous system where it regulates critical axonal growth
                      processes during guidance, filopodia formation, and
                      branching. However, little is known regarding its role in
                      synapses and the signaling events regulating PLPPR3
                      function. Here, we identify 26 high-confidence
                      phosphorylation sites in the intracellular domain of PLPPR3
                      using mass spectrometry. Biochemical characterization
                      established one of these—S351—as a bona fide
                      phosphorylation site of protein kinase A (PKA). PLPPR3 is
                      enriched at presynaptic terminals, and deletion of PLPPR3
                      results in increased depolarization-induced synaptic vesicle
                      release in hippocampal neurons. This tonic inhibitory signal
                      toward depolarization-induced presynaptic activity is
                      corrected by expression of PLPPR3 intracellular domain, but
                      not a S351A phospho-dead mutant, in Plppr3−/−
                      hippocampal neurons. We propose that PLPPR3 phosphorylation
                      under the control of PKA activity is a signaling integrator
                      of presynaptic activity in hippocampal neurons.},
      cin          = {AG Milovanovic (Berlin)},
      ddc          = {050},
      cid          = {I:(DE-2719)1813002},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:41054519},
      doi          = {10.1016/j.isci.2025.113435},
      url          = {https://pub.dzne.de/record/281370},
}