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@ARTICLE{Ogunmowo:280240,
      author       = {Ogunmowo, Tyler H and Hoffmann, Christian and Patel,
                      Chintan and Pepper, Renee and Wang, Han and Gowrisankaran,
                      Sindhuja and Idel, Johanna and Ho, Annie and Raychaudhuri,
                      Sumana and Maher, Brady J and Cooper, Benjamin H and
                      Milosevic, Ira and Milovanovic, Dragomir and Watanabe,
                      Shigeki},
      title        = {{I}ntersectin and endophilin condensates prime synaptic
                      vesicles for release site replenishment.},
      journal      = {Nature neuroscience},
      volume       = {28},
      number       = {8},
      issn         = {1097-6256},
      address      = {New York, NY},
      publisher    = {Nature America},
      reportid     = {DZNE-2025-00918},
      pages        = {1649 - 1662},
      year         = {2025},
      abstract     = {Following synaptic vesicle fusion, vacated release sites
                      are replenished immediately by new vesicles for subsequent
                      neurotransmission. These replacement vesicles are assumed to
                      be located near release sites and used by chance. Here we
                      find in mouse hippocampal excitatory synapses that
                      replacement vesicles are clustered near the active zone
                      where release sites reside by intersectin-1. Specifically,
                      intersectin-1 forms dynamic molecular condensates with
                      endophilin A1 and sequesters vesicles around this region. In
                      the absence of intersectin-1, fewer vesicles cluster within
                      20 nm of the plasma membrane, and consequently vacated sites
                      cannot be replenished rapidly, leading to synaptic
                      depression. Mutations in intersectin-1 that disrupt
                      endophilin A1 binding result in similar phenotypes. In the
                      absence of endophilin A1, intersectin-1 is mislocalized, and
                      this replacement pool of vesicles cannot be accessed,
                      suggesting that endophilin A1 is needed to mobilize these
                      vesicles. Thus, our work describes the replacement zone
                      within a synapse, where replacement vesicles are stored for
                      replenishment of the release site.},
      keywords     = {Animals / Synaptic Vesicles: metabolism / Synaptic
                      Vesicles: ultrastructure / Synaptic Vesicles: physiology /
                      Mice / Hippocampus: cytology / Hippocampus: metabolism /
                      Adaptor Proteins, Vesicular Transport: metabolism / Adaptor
                      Proteins, Vesicular Transport: genetics / Synapses:
                      metabolism / Synapses: ultrastructure / Neurons / Adaptor
                      Proteins, Signal Transducing: metabolism / Adaptor Proteins,
                      Signal Transducing: genetics / Synaptic Transmission:
                      physiology / Mice, Inbred C57BL / Mutation: genetics /
                      Adaptor Proteins, Vesicular Transport (NLM Chemicals) /
                      intersectin 1 (NLM Chemicals) / endophilin A1 protein, mouse
                      (NLM Chemicals) / Adaptor Proteins, Signal Transducing (NLM
                      Chemicals)},
      cin          = {AG Milovanovic (Berlin) / AG Milovanovic (Bonn)},
      ddc          = {610},
      cid          = {I:(DE-2719)1813002 / I:(DE-2719)1013043},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40629141},
      pmc          = {pmc:PMC12321584},
      doi          = {10.1038/s41593-025-02002-4},
      url          = {https://pub.dzne.de/record/280240},
}