% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Katsinelos:136033,
      author       = {T. Katsinelos$^*$ and M. Zeitler and E. Dimou and A.
                      Karakatsani and H.-M. Müller and E. Nachman$^*$ and J. P.
                      Steringer and C. Ruiz de Almodovar and W. Nickel and T.
                      Jahn$^*$},
      title        = {{U}nconventional {S}ecretion {M}ediates the
                      {T}rans-cellular {S}preading of {T}au.},
      journal      = {Cell reports},
      volume       = {23},
      number       = {7},
      issn         = {2211-1247},
      address      = {Maryland Heights, MO},
      publisher    = {Cell Press},
      reportid     = {DKFZ-2018-00732},
      pages        = {2039 - 2055},
      year         = {2018},
      note         = {DKFZ-ZMBH-Allianz},
      abstract     = {The progressive deposition of misfolded hyperphosphorylated
                      tau is a pathological hallmark of tauopathies, including
                      Alzheimer's disease. However, the underlying molecular
                      mechanisms governing the intercellular spreading of tau
                      species remain elusive. Here, we show that full-length
                      soluble tau is unconventionally secreted by direct
                      translocation across the plasma membrane. Increased
                      secretion is favored by tau hyperphosphorylation, which
                      provokes microtubule detachment and increases the
                      availability of free protein inside cells. Using a series of
                      binding assays, we show that free tau interacts with
                      components enriched at the inner leaflet of the plasma
                      membrane, finally leading to its translocation across the
                      plasma membrane mediated by sulfated proteoglycans. We
                      provide further evidence that secreted soluble tau species
                      spread trans-cellularly and are sufficient for the induction
                      of intracellular tau aggregation in adjacent cells. Our
                      study demonstrates the mechanistic details of tau secretion
                      and provides insights into the initiation and progression of
                      tau pathology.},
      cin          = {B180},
      ddc          = {570},
      cid          = {I:(DE-He78)B180-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29768203},
      doi          = {10.1016/j.celrep.2018.04.056},
      url          = {https://inrepo02.dkfz.de/record/136033},
}