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@ARTICLE{Jung:263974,
      author       = {Jung, Raimund and Lechler, Marie and Fernandez-Villegas,
                      Ana and Chung, Chyi Wei and Jones, Harry C and Choi, Yoon
                      Hee and Thompson, Maximilian A and Rödelsperger, Christian
                      and Röseler, Waltraud and Kaminski Schierle, Gabriele S and
                      Sommer, Ralf J and David, Della},
      title        = {{A} safety mechanism enables tissue-specific resistance to
                      protein aggregation during aging in {C}. elegans.},
      journal      = {PLoS biology},
      volume       = {21},
      number       = {9},
      issn         = {1544-9173},
      address      = {Lawrence, KS},
      publisher    = {PLoS},
      reportid     = {DZNE-2023-00908},
      pages        = {e3002284},
      year         = {2023},
      abstract     = {During aging, proteostasis capacity declines and distinct
                      proteins become unstable and can accumulate as protein
                      aggregates inside and outside of cells. Both in disease and
                      during aging, proteins selectively aggregate in certain
                      tissues and not others. Yet, tissue-specific regulation of
                      cytoplasmic protein aggregation remains poorly understood.
                      Surprisingly, we found that the inhibition of 3 core protein
                      quality control systems, namely chaperones, the proteasome,
                      and macroautophagy, leads to lower levels of age-dependent
                      protein aggregation in Caenorhabditis elegans pharyngeal
                      muscles, but higher levels in body-wall muscles. We describe
                      a novel safety mechanism that selectively targets newly
                      synthesized proteins to suppress their aggregation and
                      associated proteotoxicity. The safety mechanism relies on
                      macroautophagy-independent lysosomal degradation and
                      involves several previously uncharacterized components of
                      the intracellular pathogen response (IPR). We propose that
                      this protective mechanism engages an anti-aggregation
                      machinery targeting aggregating proteins for lysosomal
                      degradation.},
      keywords     = {Animals / Caenorhabditis elegans / Protein Aggregates /
                      Aging / Proteasome Endopeptidase Complex / Proteostasis /
                      Protein Aggregates (NLM Chemicals) / Proteasome
                      Endopeptidase Complex (NLM Chemicals)},
      cin          = {AG David},
      ddc          = {610},
      cid          = {I:(DE-2719)1210004},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC10501630},
      pubmed       = {pmid:37708127},
      doi          = {10.1371/journal.pbio.3002284},
      url          = {https://pub.dzne.de/record/263974},
}