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@ARTICLE{Hochmair:280247,
      author       = {Hochmair, Janine and van den Oetelaar, Maxime C M and
                      Ravatt, Leandre and Diez, Lisa and Lemmens, Lenne J M and
                      Ponce-Lina, Renata and Sankar, Rithika and Franck,
                      Maximilian and Nolte, Gesa and Semenova, Ekaterina and
                      Mohapatra, Satabdee and Ottmann, Christian and Brunsveld,
                      Luc and Wegmann, Susanne},
      title        = {{S}toichiometric 14-3-3ζ binding promotes phospho-{T}au
                      microtubule dissociation and reduces aggregation and
                      condensation.},
      journal      = {Communications biology},
      volume       = {8},
      number       = {1},
      issn         = {2399-3642},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {DZNE-2025-00925},
      pages        = {1139},
      year         = {2025},
      abstract     = {The microtubule (MT) association of protein Tau is
                      decreased upon phosphorylation. Increased levels of
                      phosphorylated Tau in the cytosol pose the risk of
                      pathological aggregation, as observed in neurodegenerative
                      diseases. We show that binding of 14-3-3ζ enhances
                      cytosolic Tau solubility by promoting phosphorylated Tau
                      removal from MTs, while simultaneously inhibiting Tau
                      aggregation both directly and indirectly via suppression of
                      condensate formation. These 14-3-3ζ activities depend on
                      site-specific binding of 14-3-3 to Tau phosphorylated at
                      S214 and S324. At sub-stoichiometric 14-3-3ζ
                      concentrations, or in the presence of other 14-3-3ζ binding
                      partners, multivalent electrostatic interactions promote
                      Tau:14-3-3ζ co-condensation, offering a
                      phosphorylation-independent mode of Tau-14-3-3ζ
                      interactions. Given the high abundance of 14-3-3 proteins in
                      the brain, 14-3-3 binding could provide efficient
                      multi-modal chaperoning activity for Tau in the healthy
                      brain and be important for preventing Tau aggregation in
                      disease.},
      keywords     = {14-3-3 Proteins: metabolism / tau Proteins: metabolism /
                      tau Proteins: chemistry / Microtubules: metabolism / Humans
                      / Phosphorylation / Protein Binding / Protein Aggregates /
                      Protein Aggregation, Pathological: metabolism / 14-3-3
                      Proteins (NLM Chemicals) / tau Proteins (NLM Chemicals) /
                      Protein Aggregates (NLM Chemicals) / MAPT protein, human
                      (NLM Chemicals)},
      cin          = {AG Wegmann},
      ddc          = {570},
      cid          = {I:(DE-2719)1810006},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40745206},
      pmc          = {pmc:PMC12313985},
      doi          = {10.1038/s42003-025-08548-0},
      url          = {https://pub.dzne.de/record/280247},
}