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@ARTICLE{Hoffmann:265756,
      author       = {Hoffmann, Christian and Rentsch, Jakob and Tsunoyama, Taka
                      A and Chhabra, Akshita and Aguilar Perez, Gerard and
                      Chowdhury, Rajdeep and Trnka, Franziska and Korobeinikov,
                      Aleksandr and Shaib, Ali H and Ganzella, Marcelo and
                      Giannone, Gregory and Rizzoli, Silvio O and Kusumi, Akihiro
                      and Ewers, Helge and Milovanovic, Dragomir},
      title        = {{S}ynapsin condensation controls synaptic vesicle
                      sequestering and dynamics.},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DZNE-2023-01031},
      pages        = {6730},
      year         = {2023},
      abstract     = {Neuronal transmission relies on the regulated secretion of
                      neurotransmitters, which are packed in synaptic vesicles
                      (SVs). Hundreds of SVs accumulate at synaptic boutons.
                      Despite being held together, SVs are highly mobile, so that
                      they can be recruited to the plasma membrane for their rapid
                      release during neuronal activity. However, how such
                      confinement of SVs corroborates with their motility remains
                      unclear. To bridge this gap, we employ ultrafast
                      single-molecule tracking (SMT) in the reconstituted system
                      of native SVs and in living neurons. SVs and synapsin 1, the
                      most highly abundant synaptic protein, form condensates with
                      liquid-like properties. In these condensates, synapsin 1
                      movement is slowed in both at short (i.e., 60-nm) and long
                      (i.e., several hundred-nm) ranges, suggesting that the
                      SV-synapsin 1 interaction raises the overall packing of the
                      condensate. Furthermore, two-color SMT and super-resolution
                      imaging in living axons demonstrate that synapsin 1 drives
                      the accumulation of SVs in boutons. Even the short
                      intrinsically-disordered fragment of synapsin 1 was
                      sufficient to restore the native SV motility pattern in
                      synapsin triple knock-out animals. Thus, synapsin 1
                      condensation is sufficient to guarantee reliable confinement
                      and motility of SVs, allowing for the formation of mesoscale
                      domains of SVs at synapses in vivo.},
      keywords     = {Animals / Synaptic Vesicles: metabolism / Synapsins:
                      genetics / Synapsins: metabolism / Synapses: metabolism /
                      Synaptic Transmission: physiology / Animals, Genetically
                      Modified / Synapsins (NLM Chemicals)},
      cin          = {AG Milovanovic},
      ddc          = {500},
      cid          = {I:(DE-2719)1813002},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC10593750},
      pubmed       = {pmid:37872159},
      doi          = {10.1038/s41467-023-42372-6},
      url          = {https://pub.dzne.de/record/265756},
}