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@ARTICLE{AndresAlonso:259698,
      author       = {Andres-Alonso, Maria and Borgmeyer, Maximilian and
                      Mirzapourdelavar, Hadi and Lormann, Jakob and Klein, Kim and
                      Schweizer, Michaela and Hoffmeister-Ullerich, Sabine and
                      Oelschlegel, Anja Maria and Dityatev, Alexander and Kreutz,
                      Michael R},
      title        = {{G}olgi satellites are essential for polysialylation of
                      {NCAM} and expression of {LTP} at distal synapses.},
      journal      = {Cell reports},
      volume       = {42},
      number       = {7},
      issn         = {2211-1247},
      address      = {[New York, NY]},
      publisher    = {Elsevier},
      reportid     = {DZNE-2023-00770},
      pages        = {112692},
      year         = {2023},
      abstract     = {The complex cytoarchitecture of neurons poses significant
                      challenges for the maturation of synaptic membrane proteins.
                      It is currently unclear whether locally secreted synaptic
                      proteins bypass the Golgi or whether they traffic through
                      Golgi satellites (GSs). Here, we create a transgenic GS
                      reporter mouse line and show that GSs are widely distributed
                      along dendrites and are capable of mature glycosylation, in
                      particular sialylation. We find that polysialylation of
                      locally secreted NCAM takes place at GSs. Accordingly, in
                      mice lacking a component of trans-Golgi network-to-plasma
                      membrane trafficking, we find fewer GSs and significantly
                      reduced PSA-NCAM levels in distal dendrites of CA1 neurons
                      that receive input from the temporoammonic pathway.
                      Induction of long-term potentiation at those, but not more
                      proximal, synapses is severely impaired. We conclude that
                      GSs serve the need for local mature glycosylation of
                      synaptic membrane proteins in distal dendrites and thereby
                      contribute to rapid changes in synaptic strength.},
      keywords     = {Mice / Animals / Long-Term Potentiation: physiology /
                      Synapses: metabolism / Neurons: metabolism / Dendrites:
                      metabolism / Neural Cell Adhesion Molecules: metabolism /
                      CP: Cell biology (Other) / CP: Neuroscience (Other) / Golgi
                      satellites (Other) / NCAM (Other) / polysialylation (Other)
                      / secretory trafficking (Other) / synaptic plasticity
                      (Other) / Neural Cell Adhesion Molecules (NLM Chemicals)},
      cin          = {AG Düzel / AG Dityatev},
      ddc          = {610},
      cid          = {I:(DE-2719)5000006 / I:(DE-2719)1310007},
      pnm          = {353 - Clinical and Health Care Research (POF4-353) / 351 -
                      Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-353 / G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37355986},
      doi          = {10.1016/j.celrep.2023.112692},
      url          = {https://pub.dzne.de/record/259698},
}