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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
2008-5-14
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-10428762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-10590837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-11525245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-11805121,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-11959102,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-11988737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-12089340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-12122205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-12529635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-12750521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-12882326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-14685248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-14685250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-14990998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-15036203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-15084750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-15894607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-16469881,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-16814508,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-16902091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-16973439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-17276341,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-17392428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-17401151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-6893047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-7353015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18467495-7568134
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1091-6490
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
13
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7094-9
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pubmed:dateRevised |
2011-7-11
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pubmed:meshHeading |
pubmed-meshheading:18467495-Adaptation, Physiological,
pubmed-meshheading:18467495-Animals,
pubmed-meshheading:18467495-Arsenites,
pubmed-meshheading:18467495-Caenorhabditis elegans,
pubmed-meshheading:18467495-Caenorhabditis elegans Proteins,
pubmed-meshheading:18467495-Cell Line,
pubmed-meshheading:18467495-Endoplasmic Reticulum,
pubmed-meshheading:18467495-Environment,
pubmed-meshheading:18467495-Humans,
pubmed-meshheading:18467495-Intracellular Membranes,
pubmed-meshheading:18467495-Longevity,
pubmed-meshheading:18467495-Mice,
pubmed-meshheading:18467495-Phenotype,
pubmed-meshheading:18467495-Proteasome Endopeptidase Complex,
pubmed-meshheading:18467495-Protein Binding,
pubmed-meshheading:18467495-Protein Folding,
pubmed-meshheading:18467495-RNA-Binding Proteins,
pubmed-meshheading:18467495-Sequence Homology, Amino Acid
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pubmed:year |
2008
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pubmed:articleTitle |
Proteasomal adaptation to environmental stress links resistance to proteotoxicity with longevity in Caenorhabditis elegans.
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pubmed:affiliation |
The Kimmel Center for Biology and Medicine at the Skirball Institute for Biomolecular Medicine.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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