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@ARTICLE{Schmerl:163742,
      author       = {Schmerl, Bettina and Gimber, Niclas and Kuropka, Benno and
                      Stumpf, Alexander and Rentsch, Jakob and Kunde, Stella-Amrei
                      and von Sivers, Judith and Ewers, Helge and Schmitz, Dietmar
                      and Freund, Christian and Schmoranzer, Jan and Rademacher,
                      Nils and Shoichet, Sarah A},
      title        = {{T}he synaptic scaffold protein {MPP}2 interacts with
                      {GABAA} receptors at the periphery of the postsynaptic
                      density of glutamatergic synapses.},
      journal      = {PLoS biology},
      volume       = {20},
      number       = {3},
      issn         = {1544-9173},
      address      = {Lawrence, KS},
      publisher    = {PLoS},
      reportid     = {DZNE-2022-00481},
      pages        = {e3001503},
      year         = {2022},
      abstract     = {Recent advances in imaging technology have highlighted that
                      scaffold proteins and receptors are arranged in subsynaptic
                      nanodomains. The synaptic membrane-associated guanylate
                      kinase (MAGUK) scaffold protein membrane protein
                      palmitoylated 2 (MPP2) is a component of
                      α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)
                      receptor-associated protein complexes and also binds to the
                      synaptic cell adhesion molecule SynCAM 1. Using
                      superresolution imaging, we show that-like SynCAM 1-MPP2 is
                      situated at the periphery of the postsynaptic density (PSD).
                      In order to explore MPP2-associated protein complexes, we
                      used a quantitative comparative proteomics approach and
                      identified multiple γ-aminobutyric acid (GABA)A receptor
                      subunits among novel synaptic MPP2 interactors. In line with
                      a scaffold function for MPP2 in the assembly and/or
                      modulation of intact GABAA receptors, manipulating MPP2
                      expression had effects on inhibitory synaptic transmission.
                      We further show that GABAA receptors are found together with
                      MPP2 in a subset of dendritic spines and thus highlight MPP2
                      as a scaffold that serves as an adaptor molecule, linking
                      peripheral synaptic elements critical for inhibitory
                      regulation to central structures at the PSD of glutamatergic
                      synapses.},
      keywords     = {Membrane Proteins: metabolism / Post-Synaptic Density:
                      metabolism / Receptors, AMPA: metabolism / Receptors, GABA-A
                      / Synapses: metabolism / Membrane Proteins (NLM Chemicals) /
                      Receptors, AMPA (NLM Chemicals) / Receptors, GABA-A (NLM
                      Chemicals)},
      cin          = {AG Schmitz 1 / AG Garner},
      ddc          = {610},
      cid          = {I:(DE-2719)1810004 / I:(DE-2719)1810001},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:35312684},
      pmc          = {pmc:PMC8970474},
      doi          = {10.1371/journal.pbio.3001503},
      url          = {https://pub.dzne.de/record/163742},
}