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000139113 0247_ $$2pmid$$apmid:28076789
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000139113 0247_ $$2ISSN$$a2639-1856
000139113 037__ $$aDZNE-2020-05435
000139113 041__ $$aEnglish
000139113 082__ $$a610
000139113 1001_ $$0P:(DE-2719)2810617$$aLechler, Marie C$$b0$$eFirst author$$udzne
000139113 245__ $$aReduced Insulin/IGF-1 Signaling Restores the Dynamic Properties of Key Stress Granule Proteins during Aging.
000139113 260__ $$a[New York, NY]$$bElsevier$$c2017
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000139113 520__ $$aLow-complexity 'prion-like' domains in key RNA-binding proteins (RBPs) mediate the reversible assembly of RNA granules. Individual RBPs harboring these domains have been linked to specific neurodegenerative diseases. Although their aggregation in neurodegeneration has been extensively characterized, it remains unknown how the process of aging disturbs RBP dynamics. We show that a wide variety of RNA granule components, including stress granule proteins, become highly insoluble with age in C. elegans and that reduced insulin/insulin-like growth factor 1 (IGF-1) daf-2 receptor signaling efficiently prevents their aggregation. Importantly, stress-granule-related RBP aggregates are associated with reduced fitness. We show that heat shock transcription factor 1 (HSF-1) is a main regulator of stress-granule-related RBP aggregation in both young and aged animals. During aging, increasing DAF-16 activity restores dynamic stress-granule-related RBPs, partly by decreasing the buildup of other misfolded proteins that seed RBP aggregation. Longevity-associated mechanisms found to maintain dynamic RBPs during aging could be relevant for neurodegenerative diseases.
000139113 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
000139113 542__ $$2Crossref$$i2017-01-01$$uhttps://www.elsevier.com/tdm/userlicense/1.0/
000139113 542__ $$2Crossref$$i2016-12-13$$uhttp://creativecommons.org/licenses/by-nc-nd/4.0/
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000139113 650_7 $$2NLM Chemicals$$aCaenorhabditis elegans Proteins
000139113 650_7 $$2NLM Chemicals$$aHeat-Shock Proteins
000139113 650_7 $$2NLM Chemicals$$aInsulin
000139113 650_7 $$2NLM Chemicals$$aProtein Aggregates
000139113 650_7 $$2NLM Chemicals$$aRNA-Binding Proteins
000139113 650_7 $$063231-63-0$$2NLM Chemicals$$aRNA
000139113 650_7 $$067763-96-6$$2NLM Chemicals$$aInsulin-Like Growth Factor I
000139113 650_7 $$0EC 2.7.10.1$$2NLM Chemicals$$aDAF-2 protein, C elegans
000139113 650_7 $$0EC 2.7.10.1$$2NLM Chemicals$$aReceptor, Insulin
000139113 650_2 $$2MeSH$$aAging: metabolism
000139113 650_2 $$2MeSH$$aAnimals
000139113 650_2 $$2MeSH$$aCaenorhabditis elegans: metabolism
000139113 650_2 $$2MeSH$$aCaenorhabditis elegans Proteins: metabolism
000139113 650_2 $$2MeSH$$aCytoplasmic Granules: metabolism
000139113 650_2 $$2MeSH$$aHeat-Shock Proteins: metabolism
000139113 650_2 $$2MeSH$$aInsulin: metabolism
000139113 650_2 $$2MeSH$$aInsulin-Like Growth Factor I: metabolism
000139113 650_2 $$2MeSH$$aLongevity
000139113 650_2 $$2MeSH$$aMutation: genetics
000139113 650_2 $$2MeSH$$aProtein Aggregates
000139113 650_2 $$2MeSH$$aRNA: metabolism
000139113 650_2 $$2MeSH$$aRNA-Binding Proteins: metabolism
000139113 650_2 $$2MeSH$$aReceptor, Insulin: metabolism
000139113 650_2 $$2MeSH$$aSignal Transduction
000139113 650_2 $$2MeSH$$aSolubility
000139113 7001_ $$0P:(DE-2719)2810675$$aCrawford, Emily D$$b1$$udzne
000139113 7001_ $$0P:(DE-2719)2811001$$aGroh, Nicole$$b2$$udzne
000139113 7001_ $$0P:(DE-2719)2810812$$aWidmaier, Katja$$b3$$udzne
000139113 7001_ $$0P:(DE-2719)2811479$$aJung, Raimund$$b4$$udzne
000139113 7001_ $$aKirstein, Janine$$b5
000139113 7001_ $$aTrinidad, Jonathan C$$b6
000139113 7001_ $$aBurlingame, Alma L$$b7
000139113 7001_ $$0P:(DE-2719)2810353$$aDavid, Della$$b8$$eLast author$$udzne
000139113 77318 $$2Crossref$$3journal-article$$a10.1016/j.celrep.2016.12.033$$b : Elsevier BV, 2017-01-01$$n2$$p454-467$$tCell Reports$$v18$$x2211-1247$$y2017
000139113 773__ $$0PERI:(DE-600)2649101-1$$a10.1016/j.celrep.2016.12.033$$gVol. 18, no. 2, p. 454 - 467$$n2$$p454-467$$q18:2<454 - 467$$tCell reports$$v18$$x2211-1247$$y2017
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000139113 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC5263236
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