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@ARTICLE{Katsinelos:169396,
      author       = {T. Katsinelos$^*$ and W. A. McEwan and T. Jahn$^*$ and W.
                      Nickel},
      title        = {{I}dentification of cis-acting determinants mediating the
                      unconventional secretion of tau.},
      journal      = {Scientific reports},
      volume       = {11},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {DKFZ-2021-01470},
      pages        = {12946},
      year         = {2021},
      note         = {#EA:B180#},
      abstract     = {The deposition of tau aggregates throughout the brain is a
                      pathological characteristic within a group of
                      neurodegenerative diseases collectively termed tauopathies,
                      which includes Alzheimer's disease. While recent findings
                      suggest the involvement of unconventional secretory pathways
                      driving tau into the extracellular space and mediating the
                      propagation of the disease-associated pathology, many of the
                      mechanistic details governing this process remain elusive.
                      In the current study, we provide an in-depth
                      characterization of the unconventional secretory pathway of
                      tau and identify novel molecular determinants that are
                      required for this process. Here, using Drosophila models of
                      tauopathy, we correlate the hyperphosphorylation and
                      aggregation state of tau with the disease-related
                      neurotoxicity. These newly established systems recapitulate
                      all the previously identified hallmarks of tau secretion,
                      including the contribution of tau hyperphosphorylation as
                      well as the requirement for PI(4,5)P2 triggering the direct
                      translocation of tau. Using a series of cellular assays, we
                      demonstrate that both the sulfated proteoglycans on the cell
                      surface and the correct orientation of the protein at the
                      inner plasma membrane leaflet are critical determinants of
                      this process. Finally, we identify two cysteine residues
                      within the microtubule binding repeat domain as novel
                      cis-elements that are important for both unconventional
                      secretion and trans-cellular propagation of tau.},
      cin          = {B180},
      ddc          = {600},
      cid          = {I:(DE-He78)B180-20160331},
      pnm          = {312 - Funktionelle und strukturelle Genomforschung
                      (POF4-312)},
      pid          = {G:(DE-HGF)POF4-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34155306},
      pmc          = {pmc:PMC8217235},
      doi          = {10.1038/s41598-021-92433-3},
      url          = {https://inrepo02.dkfz.de/record/169396},
}