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@ARTICLE{Gundelfinger:163766,
      author       = {Gundelfinger, Eckart D and Karpova, Anna and Pielot, Rainer
                      and Garner, Craig C. and Kreutz, Michael R.},
      title        = {{O}rganization of {P}resynaptic {A}utophagy-{R}elated
                      {P}rocesses},
      journal      = {Frontiers in synaptic neuroscience},
      volume       = {14},
      issn         = {1663-3563},
      address      = {Lausanne},
      publisher    = {Frontiers Research Foundation},
      reportid     = {DZNE-2022-00505},
      pages        = {829354},
      year         = {2022},
      abstract     = {Brain synapses pose special challenges on the quality
                      control of their protein machineries as they are far away
                      from the neuronal soma, display a high potential for plastic
                      adaptation and have a high energy demand to fulfill their
                      physiological tasks. This applies in particular to the
                      presynaptic part where neurotransmitter is released from
                      synaptic vesicles, which in turn have to be recycled and
                      refilled in a complex membrane trafficking cycle. Pathways
                      to remove outdated and damaged proteins include the
                      ubiquitin-proteasome system acting in the cytoplasm as well
                      as membrane-associated endolysosomal and the autophagy
                      systems. Here we focus on the latter systems and review what
                      is known about the spatial organization of autophagy and
                      endolysomal processes within the presynapse. We provide an
                      inventory of which components of these degradative systems
                      were found to be present in presynaptic boutons and where
                      they might be anchored to the presynaptic apparatus. We
                      identify three presynaptic structures reported to interact
                      with known constituents of membrane-based
                      protein-degradation pathways and therefore may serve as
                      docking stations. These are (i) scaffolding proteins of the
                      cytomatrix at the active zone, such as Bassoon or Clarinet,
                      (ii) the endocytic machinery localized mainly at the
                      peri-active zone, and (iii) synaptic vesicles. Finally, we
                      sketch scenarios, how presynaptic autophagic cargos are
                      tagged and recruited and which cellular mechanisms may
                      govern membrane-associated protein turnover in the
                      presynapse.},
      subtyp        = {Review Article},
      cin          = {AG Düzel / AG Garner},
      ddc          = {610},
      cid          = {I:(DE-2719)5000006 / I:(DE-2719)1810001},
      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},
      pmc          = {pmc:PMC8968026},
      pubmed       = {pmid:35368245},
      doi          = {10.3389/fnsyn.2022.829354},
      url          = {https://pub.dzne.de/record/163766},
}