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@ARTICLE{Lechler:139113,
      author       = {Lechler, Marie C and Crawford, Emily D and Groh, Nicole and
                      Widmaier, Katja and Jung, Raimund and Kirstein, Janine and
                      Trinidad, Jonathan C and Burlingame, Alma L and David,
                      Della},
      title        = {{R}educed {I}nsulin/{IGF}-1 {S}ignaling {R}estores the
                      {D}ynamic {P}roperties of {K}ey {S}tress {G}ranule
                      {P}roteins during {A}ging.},
      journal      = {Cell reports},
      volume       = {18},
      number       = {2},
      issn         = {2211-1247},
      address      = {[New York, NY]},
      publisher    = {Elsevier},
      reportid     = {DZNE-2020-05435},
      pages        = {454-467},
      year         = {2017},
      abstract     = {Low-complexity 'prion-like' domains in key RNA-binding
                      proteins (RBPs) mediate the reversible assembly of RNA
                      granules. Individual RBPs harboring these domains have been
                      linked to specific neurodegenerative diseases. Although
                      their aggregation in neurodegeneration has been extensively
                      characterized, it remains unknown how the process of aging
                      disturbs RBP dynamics. We show that a wide variety of RNA
                      granule components, including stress granule proteins,
                      become highly insoluble with age in C. elegans and that
                      reduced insulin/insulin-like growth factor 1 (IGF-1) daf-2
                      receptor signaling efficiently prevents their aggregation.
                      Importantly, stress-granule-related RBP aggregates are
                      associated with reduced fitness. We show that heat shock
                      transcription factor 1 (HSF-1) is a main regulator of
                      stress-granule-related RBP aggregation in both young and
                      aged animals. During aging, increasing DAF-16 activity
                      restores dynamic stress-granule-related RBPs, partly by
                      decreasing the buildup of other misfolded proteins that seed
                      RBP aggregation. Longevity-associated mechanisms found to
                      maintain dynamic RBPs during aging could be relevant for
                      neurodegenerative diseases.},
      keywords     = {Aging: metabolism / Animals / Caenorhabditis elegans:
                      metabolism / Caenorhabditis elegans Proteins: metabolism /
                      Cytoplasmic Granules: metabolism / Heat-Shock Proteins:
                      metabolism / Insulin: metabolism / Insulin-Like Growth
                      Factor I: metabolism / Longevity / Mutation: genetics /
                      Protein Aggregates / RNA: metabolism / RNA-Binding Proteins:
                      metabolism / Receptor, Insulin: metabolism / Signal
                      Transduction / Solubility / Caenorhabditis elegans Proteins
                      (NLM Chemicals) / Heat-Shock Proteins (NLM Chemicals) /
                      Insulin (NLM Chemicals) / Protein Aggregates (NLM Chemicals)
                      / RNA-Binding Proteins (NLM Chemicals) / RNA (NLM Chemicals)
                      / Insulin-Like Growth Factor I (NLM Chemicals) / DAF-2
                      protein, C elegans (NLM Chemicals) / Receptor, Insulin (NLM
                      Chemicals)},
      cin          = {AG David},
      ddc          = {610},
      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},
      pubmed       = {pmid:28076789},
      pmc          = {pmc:PMC5263236},
      doi          = {10.1016/j.celrep.2016.12.033},
      url          = {https://pub.dzne.de/record/139113},
}