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@ARTICLE{Chhabra:281358,
      author       = {Chhabra, Akshita and Hoffmann, Christian and Aguilar Perez,
                      Gerard and Korobeinikov, Aleksandr A and Rentsch, Jakob and
                      Hümpfer, Nadja and Kokwaro, Linda and Gnidovec, Luka and
                      Petrović, Arsen and Wallace, Jaqulin N and Tromm, Johannes
                      Vincent and Román-Vendrell, Cristina and Johnson, Emma C
                      and Ranković, Branislava and Perego, Eleonora and Volpi,
                      Tommaso and Fernández-Busnadiego, Rubén and Köster, Sarah
                      and Rizzoli, Silvio O and Ewers, Helge and Morgan, Jennifer
                      R and Milovanovic, Dragomir},
      title        = {{C}ondensates of synaptic vesicles and synapsin-1 mediate
                      actin sequestering and polymerization.},
      journal      = {The EMBO journal},
      volume       = {44},
      number       = {18},
      issn         = {0261-4189},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DZNE-2025-01105},
      pages        = {5112 - 5148},
      year         = {2025},
      abstract     = {Neuronal communication relies on precisely maintained
                      synaptic vesicle (SV) clusters, which assemble via
                      liquid-liquid phase separation. This process requires
                      synapsins, the major synaptic phosphoproteins, which are
                      known to bind actin. Reorganization of SVs, synapsins, and
                      actin is a hallmark of synaptic activity, but the molecular
                      details of the interactions between these components remain
                      unclear. Here, we combine in vitro reconstitution with
                      expansion microscopy, super-resolution imaging, and
                      cryo-electron tomography to dissect the roles of
                      SV-synapsin-1 condensates in the organization of the
                      presynaptic actin cytoskeleton. Our results indicate that
                      condensation of synapsin-1 initiates actin polymerization.
                      This process enables SV-synapsin-actin assemblies to
                      facilitate the mesoscale organization of SV clusters along
                      axons, which is similar to the native presynaptic
                      organization observed at both lamprey and mammalian
                      synapses. Understanding the relationship between the actin
                      network and synapsin-synaptic vesicle condensates can help
                      elucidate how coordinated neurotransmission along the axon
                      enables circuit function and behavior.},
      keywords     = {Synaptic Vesicles: metabolism / Synaptic Vesicles:
                      ultrastructure / Synapsins: metabolism / Animals / Actins:
                      metabolism / Polymerization / Actin Cytoskeleton: metabolism
                      / Synapses: metabolism / Actin (Other) / Liquid-Liquid Phase
                      Separation (Other) / Presynapses (Other) / Synapsin (Other)
                      / Synaptic Vesicles (Other) / Synapsins (NLM Chemicals) /
                      Actins (NLM Chemicals)},
      cin          = {AG Milovanovic (Berlin)},
      ddc          = {570},
      cid          = {I:(DE-2719)1813002},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40813925},
      pmc          = {pmc:PMC12436662},
      doi          = {10.1038/s44318-025-00516-y},
      url          = {https://pub.dzne.de/record/281358},
}