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Proteasomal adaptation to environmental stress links resistance to proteotoxicity with longevity in Caenorhabditis elegans.

http://www.ncbi.nlm.nih.gov/pubmed/18467495

The burden of protein misfolding is believed to contribute to aging. However, the links between adaptations to conditions associated with protein misfolding and resistance to the time-dependent attrition of cellular function remain poorly understood. We report that worms lacking aip-1, a homologue of mammalian AIRAP (arsenic-inducible proteasomal 19S regulatory particle-associated protein), are not only impaired in their ability to resist exposure to arsenite but also exhibit shortened lifespan and hypersensitivity to misfolding-prone proteins under normal laboratory conditions. Mammals have a second, constitutively expressed AIRAP-like gene (AIRAPL) that also encodes a proteasome-interacting protein, which shares with AIRAP the property of enhancing peptide accessibility to the proteasome's active site. Genetic rescue experiments suggest that features common to the constitutively expressed worm AIP-1 and mammalian AIRAPL (but missing in the smaller, arsenite-inducible AIRAP) are important to lifespan extension. In worms, a single AIRAP-related protein links proteasomal adaptation to environmental stress with resistance to both proteotoxic insults and maintenance of animal life span under normal conditions.

Pubmed ID: 18467495 RIS Download

Mesh terms: Adaptation, Physiological | Animals | Arsenites | Caenorhabditis elegans | Caenorhabditis elegans Proteins | Cell Line | Endoplasmic Reticulum | Environment | Humans | Intracellular Membranes | Longevity | Mice | Phenotype | Proteasome Endopeptidase Complex | Protein Binding | Protein Folding | RNA-Binding Proteins | Sequence Homology, Amino Acid

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Associated grants

  • Agency: NIDDK NIH HHS, Id: DK47119
  • Agency: NIEHS NIH HHS, Id: ES08681
  • Agency: NIDDK NIH HHS, Id: F32-DK61179
  • Agency: NINDS NIH HHS, Id: NS050276
  • Agency: NCRR NIH HHS, Id: RR017990

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