% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Petzoldt:480707,
      author       = {Petzoldt, Astrid G. and Götz, Torsten W. B. and Driller,
                      Jan Heiner and Lützkendorf, Janine and Reddy-Alla, Suneel
                      and Matkovic-Rachid, Tanja and Liu, Sunbin and Knoche, Elena
                      and Mertel, Sara and Ugorets, Vladimir and Lehmann, Martin
                      and Ramesh, Niraja and Beuschel, Christine Brigitte and
                      Kuropka, Benno and Freund, Christian and Stelzl, Ulrich and
                      Loll, Bernhard and Liu, Fan and Wahl, Markus C. and Sigrist,
                      Stephan J.},
      title        = {{RIM}-binding protein couples synaptic vesicle recruitment
                      to release sites},
      journal      = {The journal of cell biology},
      volume       = {219},
      number       = {7},
      issn         = {0021-9525},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PUBDB-2022-03945},
      pages        = {e201902059},
      year         = {2020},
      abstract     = {At presynaptic active zones, arrays of large conserved
                      scaffold proteins mediate fast and temporally precise
                      release of synaptic vesicles (SVs). SV release sites could
                      be identified by clusters of Munc13, which allow SVs to dock
                      in defined nanoscale relation to Ca2+ channels. We here show
                      in Drosophila that RIM-binding protein (RIM-BP) connects
                      release sites physically and functionally to the ELKS family
                      Bruchpilot (BRP)-based scaffold engaged in SV recruitment.
                      The RIM-BP N-terminal domain, while dispensable for SV
                      release site organization, was crucial for proper nanoscale
                      patterning of the BRP scaffold and needed for SV recruitment
                      of SVs under strong stimulation. Structural analysis further
                      showed that the RIM-BP fibronectin domains form a
                      “hinge” in the protein center, while the C-terminal SH3
                      domain tandem binds RIM, Munc13, and Ca2+ channels release
                      machinery collectively. RIM-BPs’ conserved domain
                      architecture seemingly provides a relay to guide SVs from
                      membrane far scaffolds into membrane close release sites.},
      cin          = {EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32369542},
      UT           = {WOS:000548271800010},
      doi          = {10.1083/jcb.201902059},
      url          = {https://bib-pubdb1.desy.de/record/480707},
}