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@ARTICLE{Wolfes:154364,
      author       = {Wolfes, Anne C and Dean, Camin},
      title        = {{T}he diversity of synaptotagmin isoforms.},
      journal      = {Current opinion in neurobiology},
      volume       = {63},
      issn         = {0959-4388},
      address      = {Philadelphia, Pa.},
      publisher    = {Current Biology},
      reportid     = {DZNE-2021-00217},
      pages        = {198 - 209},
      year         = {2020},
      note         = {ISSN 0959-4388 not unique: **3 hits**.},
      abstract     = {The synaptotagmin family of molecules is known for
                      regulating calcium-dependent membrane fusion events. Mice
                      and humans express 17 synaptotagmin isoforms, where most
                      studies have focused on isoforms 1, 2, and 7, which are
                      involved in synaptic vesicle exocytosis. Recent work has
                      highlighted how brain function relies on additional
                      isoforms, with roles in postsynaptic receptor endocytosis,
                      vesicle trafficking, membrane repair, synaptic plasticity,
                      and protection against neurodegeneration, for example, in
                      addition to the traditional concept of
                      synaptotagmin-mediated neurotransmitter release - in neurons
                      as well as glia, and at different timepoints. In fact, it is
                      not uncommon for the same isoform to feature several splice
                      isoforms, form homo- and heterodimers, and function in
                      different subcellular locations and cell types. This review
                      aims to highlight the diversity of synaptotagmins, offers a
                      concise summary of key findings on all isoforms, and
                      discusses different ways of grouping these.},
      subtyp        = {Review Article},
      keywords     = {Animals / Calcium: metabolism / Exocytosis / Humans /
                      Membrane Fusion / Mice / Nerve Tissue Proteins: metabolism /
                      Protein Isoforms: genetics / Protein Isoforms: metabolism /
                      Synaptotagmin I / Synaptotagmins: genetics / Nerve Tissue
                      Proteins (NLM Chemicals) / Protein Isoforms (NLM Chemicals)
                      / Synaptotagmin I (NLM Chemicals) / Synaptotagmins (NLM
                      Chemicals) / Calcium (NLM Chemicals)},
      cin          = {AG Dean},
      ddc          = {610},
      cid          = {I:(DE-2719)1813003},
      pnm          = {341 - Molecular Signaling (POF3-341)},
      pid          = {G:(DE-HGF)POF3-341},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32663762},
      doi          = {10.1016/j.conb.2020.04.006},
      url          = {https://pub.dzne.de/record/154364},
}