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@ARTICLE{Mller:140623,
      author       = {Müller, Tanja M and Gierke, Kaspar and Joachimsthaler,
                      Anneka and Sticht, Heinrich and Izsvák, Zsuzsanna and
                      Hamra, F Kent and Fejtová, Anna and Ackermann, Frauke and
                      Garner, Craig C and Kremers, Jan and Brandstätter, Johann H
                      and Regus-Leidig, Hanna},
      title        = {{A} {M}ultiple {P}iccolino-{RIBEYE} {I}nteraction
                      {S}upports {P}late-{S}haped {S}ynaptic {R}ibbons in
                      {R}etinal {N}eurons.},
      journal      = {The journal of neuroscience},
      volume       = {39},
      number       = {14},
      issn         = {0270-6474},
      address      = {Washington, DC},
      publisher    = {Soc.57413},
      reportid     = {DZNE-2020-06945},
      pages        = {2606-2619},
      year         = {2019},
      abstract     = {Active zones at chemical synapses are highly specialized
                      sites for the regulated release of neurotransmitters.
                      Despite a high degree of active zone protein conservation in
                      vertebrates, every type of chemical synapse expresses a
                      given set of protein isoforms and splice variants adapted to
                      the demands on neurotransmitter release. So far, we know
                      little about how specific active zone proteins contribute to
                      the structural and functional diversity of active zones. In
                      this study, we explored the nanodomain organization of
                      ribbon-type active zones by addressing the significance of
                      Piccolino, the ribbon synapse-specific splice variant of
                      Piccolo, for shaping the ribbon structure. We followed up on
                      previous results, which indicated that rod photoreceptor
                      synaptic ribbons lose their structural integrity in a
                      knockdown of Piccolino. Here, we demonstrate an interaction
                      between Piccolino and the major ribbon component RIBEYE that
                      supports plate-shaped synaptic ribbons in retinal neurons.
                      In a detailed ultrastructural analysis of three different
                      types of retinal ribbon synapses in
                      Piccolo/Piccolino-deficient male and female rats, we show
                      that the absence of Piccolino destabilizes the
                      superstructure of plate-shaped synaptic ribbons, although
                      with variable manifestation in the cell types examined. Our
                      analysis illustrates how the expression of a specific active
                      zone protein splice variant (e.g., Piccolino) contributes to
                      structural diversity of vertebrate active zones.SIGNIFICANCE
                      STATEMENT Retinal ribbon synapses are a specialized type of
                      chemical synapse adapted for the regulated fast and tonic
                      release of neurotransmitter. The hallmark of retinal ribbon
                      synapses is the plate-shaped synaptic ribbon, which extends
                      from the release site into the terminals' cytoplasm and
                      tethers hundreds of synaptic vesicles. Here, we show that
                      Piccolino, the synaptic ribbon specific splice variant of
                      Piccolo, interacts with RIBEYE, the main component of
                      synaptic ribbons. This interaction occurs via several
                      PxDLS-like motifs located at the C terminus of Piccolino,
                      which can connect multiple RIBEYE molecules. Loss of
                      Piccolino disrupts the characteristic plate-shaped structure
                      of synaptic ribbons, indicating a role of Piccolino in
                      synaptic ribbon assembly.},
      keywords     = {Alcohol Oxidoreductases: chemistry / Alcohol
                      Oxidoreductases: genetics / Alcohol Oxidoreductases:
                      metabolism / Animals / Co-Repressor Proteins: chemistry /
                      Co-Repressor Proteins: genetics / Co-Repressor Proteins:
                      metabolism / Cytoskeletal Proteins: chemistry / Cytoskeletal
                      Proteins: genetics / Cytoskeletal Proteins: metabolism /
                      HEK293 Cells / Humans / Mice / Mice, Inbred C57BL / Mice,
                      Transgenic / NIH 3T3 Cells / Neuropeptides: chemistry /
                      Neuropeptides: genetics / Neuropeptides: metabolism /
                      Protein Binding: physiology / Protein Structure, Secondary /
                      Protein Structure, Tertiary / Rats / Rats, Sprague-Dawley /
                      Rats, Transgenic / Retinal Neurons: metabolism / Retinal
                      Neurons: ultrastructure / Synapses: genetics / Synapses:
                      metabolism / Synapses: ultrastructure},
      cin          = {AG Garner / AG Ackermann},
      ddc          = {610},
      cid          = {I:(DE-2719)1810001 / I:(DE-2719)1813004},
      pnm          = {341 - Molecular Signaling (POF3-341)},
      pid          = {G:(DE-HGF)POF3-341},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30696732},
      pmc          = {pmc:PMC6445989},
      doi          = {10.1523/JNEUROSCI.2038-18.2019},
      url          = {https://pub.dzne.de/record/140623},
}