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@ARTICLE{Soykan:207421,
      author       = {Soykan, T. and Schneeberger, D. and Tria, G. and Buechner,
                      C. and Bader, N. and Svergun, D. and Tessmer, I. and
                      Poulopoulos, A. and Papadopoulos, T. and Varoqueaux, F. and
                      Schindelin, H. and Brose, N.},
      title        = {{A} {C}onformational {S}witch in {C}ollybistin {D}etermines
                      the {D}ifferentiation of {I}nhibitory {P}ostsynapses},
      journal      = {The EMBO journal},
      volume       = {33},
      number       = {18},
      issn         = {1460-2075},
      address      = {Heidelberg},
      publisher    = {EMBO Press},
      reportid     = {PUBDB-2015-01331},
      pages        = {2113 - 2133},
      year         = {2014},
      note         = {(c) The Authors},
      abstract     = {The formation of neuronal synapses and the dynamic
                      regulation of their efficacy depend on the assembly of the
                      postsynaptic neurotransmitter receptor apparatus. Receptor
                      recruitment to inhibitory GABAergic and glycinergic synapses
                      is controlled by the scaffold protein gephyrin and the
                      adaptor protein collybistin. We derived new insights into
                      the structure of collybistin and used these to design
                      biochemical, cell biological, and genetic analyses of
                      collybistin function. Our data define a collybistin‐based
                      protein interaction network that controls the gephyrin
                      content of inhibitory postsynapses. Within this network,
                      collybistin can adopt open/active and closed/inactive
                      conformations to act as a switchable adaptor that links
                      gephyrin to plasma membrane phosphoinositides. This function
                      of collybistin is regulated by binding of the adhesion
                      protein neuroligin‐2, which stabilizes the open/active
                      conformation of collybistin at the postsynaptic plasma
                      membrane by competing with an intramolecular interaction in
                      collybistin that favors the closed/inactive conformation. By
                      linking trans‐synaptic neuroligin‐dependent adhesion and
                      phosphoinositide signaling with gephyrin recruitment, the
                      collybistin‐based regulatory switch mechanism represents
                      an integrating regulatory node in the formation and function
                      of inhibitory postsynapses.},
      cin          = {EMBL / EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-20120731 / I:(DE-H253)EMBL-User-20120814},
      pnm          = {DORIS Beamline D1.2 (POF2-54G13) / EUROSPIN - European
                      Consortium on Synaptic Protein Networks in Neurological and
                      Psychiatric Diseases (241498) / SYNSYS - Synaptic Systems:
                      dissecting brain function in health and disease (242167) /
                      BIOSTRUCT-X - Transnational access and enhancement of
                      integrated Biological Structure determination at synchrotron
                      X-ray radiation facilities (283570)},
      pid          = {G:(DE-H253)POF2-D1.2-20130405 / G:(EU-Grant)241498 /
                      G:(EU-Grant)242167 / G:(EU-Grant)283570},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000342503000012},
      pubmed       = {pmid:25082542},
      doi          = {10.15252/embj.201488143},
      url          = {https://bib-pubdb1.desy.de/record/207421},
}