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@ARTICLE{Kimura:893173,
      author       = {Kimura, Kenichi and Ooms, Astrid and Graf-Riesen, Kathrin
                      and Kuppusamy, Maithreyan and Unger, Andreas and Schuld,
                      Julia and Daerr, Jan and Lother, Achim and Geisen, Caroline
                      and Hein, Lutz and Takahashi, Satoru and Li, Guang and
                      Röll, Wilhelm and Bloch, Wilhelm and van der Ven, Peter F.
                      M. and Linke, Wolfgang A. and Wu, Sean M. and Huesgen,
                      Pitter F. and Höhfeld, Jörg and Fürst, Dieter O. and
                      Fleischmann, Bernd K. and Hesse, Michael},
      title        = {{O}verexpression of human {BAG}3{P}209{L} in mice causes
                      restrictive cardiomyopathy},
      journal      = {Nature Communications},
      volume       = {12},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2021-02607},
      pages        = {3575},
      year         = {2021},
      note         = {grant ID: DFG Forschergruppe 2743 Mechanical Stress
                      Protection. DFG Projektnummer 401331881Teilprojekt 3:
                      Mechanosensoren unter Stress - Entschlüsselung der
                      Wechselwirkung zwischen Proteinentfaltung, Signalgebung und
                      Proteolyse},
      abstract     = {An amino acid exchange (P209L) in the HSPB8 binding site of
                      the human co-chaperone BAG3 gives rise to severe childhood
                      cardiomyopathy. To phenocopy the disease in mice and gain
                      insight into its mechanisms, we generated humanized
                      transgenic mouse models. Expression of human BAG3P209L-eGFP
                      in mice caused Z-disc disintegration and formation of
                      protein aggregates. This was accompanied by massive fibrosis
                      resulting in early-onset restrictive cardiomyopathy with
                      increased mortality as observed in patients. RNA-Seq and
                      proteomics revealed changes in the protein quality control
                      system and increased autophagy in hearts from
                      hBAG3P209L-eGFP mice. The mutation renders hBAG3P209L less
                      soluble in vivo and induces protein aggregation, but does
                      not abrogate hBAG3 binding properties. In conclusion, we
                      report a mouse model mimicking the human disease. Our data
                      suggest that the disease mechanism is due to accumulation of
                      hBAG3P209L and mouse Bag3, causing sequestering of
                      components of the protein quality control system and
                      autophagy machinery leading to sarcomere disruption.},
      cin          = {ZEA-3},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ZEA-3-20090406},
      pnm          = {524 - Molecular and Cellular Information Processing
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-524},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34117258},
      UT           = {WOS:000663757400001},
      doi          = {10.1038/s41467-021-23858-7},
      url          = {https://juser.fz-juelich.de/record/893173},
}