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@ARTICLE{Chakraborty:275936,
      author       = {Chakraborty, Pijush and Zweckstetter, Markus},
      title        = {{I}nterplay of p23 with {FKBP}51 and their chaperone
                      complex in regulating tau aggregation.},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {DZNE-2025-00158},
      pages        = {669},
      year         = {2025},
      abstract     = {The pathological deposition of tau and amyloid-beta into
                      insoluble amyloid fibrils are pathological hallmarks of
                      Alzheimer's disease. Molecular chaperones are important
                      cellular factors contributing to the regulation of tau
                      misfolding and aggregation. Here we reveal an
                      Hsp90-independent mechanism by which the co-chaperone p23 as
                      well as a molecular complex formed by two co-chaperones, p23
                      and FKBP51, modulates tau aggregation. Integrating NMR
                      spectroscopy, SAXS, molecular docking, and site-directed
                      mutagenesis we reveal the structural basis of the p23-FKBP51
                      complex. We show that p23 specifically recognizes the TPR
                      domain of FKBP51 and interacts with tau through its
                      C-terminal disordered tail. We further show that the
                      p23-FKBP51 complex binds tau to form a dynamic
                      p23-FKBP51-tau trimeric complex that delays tau aggregation
                      and thus may counteract Hsp90-FKBP51 mediated toxicity.
                      Taken together, our findings reveal a co-chaperone mediated
                      Hsp90-independent chaperoning of tau protein.},
      keywords     = {tau Proteins: metabolism / tau Proteins: chemistry / tau
                      Proteins: genetics / Tacrolimus Binding Proteins: metabolism
                      / Tacrolimus Binding Proteins: genetics / Humans / Molecular
                      Chaperones: metabolism / HSP90 Heat-Shock Proteins:
                      metabolism / HSP90 Heat-Shock Proteins: genetics /
                      Prostaglandin-E Synthases: metabolism / Prostaglandin-E
                      Synthases: genetics / Protein Binding / Molecular Docking
                      Simulation / Alzheimer Disease: metabolism / Alzheimer
                      Disease: genetics / Alzheimer Disease: pathology / Protein
                      Aggregates / Protein Aggregation, Pathological: metabolism /
                      Scattering, Small Angle / HSP40 Heat-Shock Proteins / tau
                      Proteins (NLM Chemicals) / Tacrolimus Binding Proteins (NLM
                      Chemicals) / tacrolimus binding protein 5 (NLM Chemicals) /
                      Molecular Chaperones (NLM Chemicals) / HSP90 Heat-Shock
                      Proteins (NLM Chemicals) / Prostaglandin-E Synthases (NLM
                      Chemicals) / MAPT protein, human (NLM Chemicals) / DNAJA1
                      protein, human (NLM Chemicals) / Protein Aggregates (NLM
                      Chemicals) / HSP40 Heat-Shock Proteins (NLM Chemicals)},
      cin          = {AG Zweckstetter},
      ddc          = {500},
      cid          = {I:(DE-2719)1410001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39809798},
      pmc          = {pmc:PMC11733250},
      doi          = {10.1038/s41467-025-56028-0},
      url          = {https://pub.dzne.de/record/275936},
}