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@ARTICLE{Lechler:139632,
      author       = {Lechler, Marie C and David, Della C},
      title        = {{M}ore stressed out with age? {C}heck your {RNA} granule
                      aggregation.},
      journal      = {Prion},
      volume       = {11},
      number       = {5},
      issn         = {1933-6896},
      address      = {London [u.a.]},
      publisher    = {Taylor $\&$ Francis},
      reportid     = {DZNE-2020-05954},
      pages        = {313-322},
      year         = {2017},
      abstract     = {Low complexity (LC) prion-like domains are over-represented
                      among RNA-binding proteins (RBPs) and contribute to the
                      dynamic nature of RNA granules. Importantly, several
                      neurodegenerative diseases are characterized by cytoplasmic
                      'solid' aggregates formed by mainly nuclear RBPs harboring
                      LC prion-like domains. Although RBP aggregation in disease
                      has been extensively characterized, it remains unknown how
                      the process of aging disturbs RBP dynamics. Our recent study
                      revealed that RNA granule components including 2 key stress
                      granule RBPs with LC prion-like domains, PAB-1 and TIAR-2,
                      aggregate in aged Caenorhabditis elegans in the absence of
                      disease. Here we present new evidence showing that sustained
                      stress granule formation triggers RBP aggregation. In
                      addition, we demonstrate that mild chronic stress during
                      aging promotes mislocalization of nuclear RBPs. We discuss
                      the consequences of aberrant interactions between
                      age-related RBP aggregation and disease-associated RBP
                      aggregation. In particular, we show that FUST-1 and PAB-1
                      co-localize in aberrant cytoplasmic accumulations.
                      Significantly, long-lived animals with reduced insulin/IGF-1
                      signaling abrogate stress granule RBP aggregation through
                      activation of the transcription factors HSF-1 and DAF-16. We
                      evaluate the different mechanisms that could maintain
                      dynamic stress granules. Together these findings highlight
                      how changes with age could contribute to pathogenesis in
                      neurodegenerative diseases and disruption of RNA
                      homeostasis.},
      keywords     = {Aging: metabolism / Animals / Caenorhabditis elegans:
                      genetics / Caenorhabditis elegans Proteins: metabolism /
                      Cytoplasmic Granules: metabolism / Forkhead Transcription
                      Factors: metabolism / Humans / Longevity / Neurodegenerative
                      Diseases: metabolism / Poly(A)-Binding Protein I: metabolism
                      / Prions: metabolism / Protein Aggregation, Pathological:
                      metabolism / Proteome: chemistry / RNA: metabolism /
                      RNA-Binding Proteins: metabolism / Stress, Physiological /
                      Transcription Factors: metabolism / Caenorhabditis elegans
                      Proteins (NLM Chemicals) / Forkhead Transcription Factors
                      (NLM Chemicals) / Poly(A)-Binding Protein I (NLM Chemicals)
                      / Prions (NLM Chemicals) / Proteome (NLM Chemicals) /
                      RNA-Binding Proteins (NLM Chemicals) / Transcription Factors
                      (NLM Chemicals) / daf-16 protein, C elegans (NLM Chemicals)
                      / heat shock factor-1, C elegans (NLM Chemicals) / RNA (NLM
                      Chemicals)},
      cin          = {AG David},
      ddc          = {570},
      cid          = {I:(DE-2719)1210004},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC7030885},
      pubmed       = {pmid:28956717},
      doi          = {10.1080/19336896.2017.1356559},
      url          = {https://pub.dzne.de/record/139632},
}