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000139632 0247_ $$2ISSN$$a1933-690X
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000139632 037__ $$aDZNE-2020-05954
000139632 041__ $$aEnglish
000139632 082__ $$a570
000139632 1001_ $$0P:(DE-2719)2810617$$aLechler, Marie C$$b0$$eFirst author$$udzne
000139632 245__ $$aMore stressed out with age? Check your RNA granule aggregation.
000139632 260__ $$aLondon [u.a.]$$bTaylor & Francis$$c2017
000139632 264_1 $$2Crossref$$3online$$bInforma UK Limited$$c2017-10-12
000139632 264_1 $$2Crossref$$3print$$bInforma UK Limited$$c2017-09-03
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000139632 520__ $$aLow complexity (LC) prion-like domains are over-represented among RNA-binding proteins (RBPs) and contribute to the dynamic nature of RNA granules. Importantly, several neurodegenerative diseases are characterized by cytoplasmic 'solid' aggregates formed by mainly nuclear RBPs harboring LC prion-like domains. Although RBP aggregation in disease has been extensively characterized, it remains unknown how the process of aging disturbs RBP dynamics. Our recent study revealed that RNA granule components including 2 key stress granule RBPs with LC prion-like domains, PAB-1 and TIAR-2, aggregate in aged Caenorhabditis elegans in the absence of disease. Here we present new evidence showing that sustained stress granule formation triggers RBP aggregation. In addition, we demonstrate that mild chronic stress during aging promotes mislocalization of nuclear RBPs. We discuss the consequences of aberrant interactions between age-related RBP aggregation and disease-associated RBP aggregation. In particular, we show that FUST-1 and PAB-1 co-localize in aberrant cytoplasmic accumulations. Significantly, long-lived animals with reduced insulin/IGF-1 signaling abrogate stress granule RBP aggregation through activation of the transcription factors HSF-1 and DAF-16. We evaluate the different mechanisms that could maintain dynamic stress granules. Together these findings highlight how changes with age could contribute to pathogenesis in neurodegenerative diseases and disruption of RNA homeostasis.
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000139632 650_7 $$2NLM Chemicals$$aCaenorhabditis elegans Proteins
000139632 650_7 $$2NLM Chemicals$$aForkhead Transcription Factors
000139632 650_7 $$2NLM Chemicals$$aPoly(A)-Binding Protein I
000139632 650_7 $$2NLM Chemicals$$aPrions
000139632 650_7 $$2NLM Chemicals$$aProteome
000139632 650_7 $$2NLM Chemicals$$aRNA-Binding Proteins
000139632 650_7 $$2NLM Chemicals$$aTranscription Factors
000139632 650_7 $$2NLM Chemicals$$adaf-16 protein, C elegans
000139632 650_7 $$2NLM Chemicals$$aheat shock factor-1, C elegans
000139632 650_7 $$063231-63-0$$2NLM Chemicals$$aRNA
000139632 650_2 $$2MeSH$$aAging: metabolism
000139632 650_2 $$2MeSH$$aAnimals
000139632 650_2 $$2MeSH$$aCaenorhabditis elegans: genetics
000139632 650_2 $$2MeSH$$aCaenorhabditis elegans Proteins: metabolism
000139632 650_2 $$2MeSH$$aCytoplasmic Granules: metabolism
000139632 650_2 $$2MeSH$$aForkhead Transcription Factors: metabolism
000139632 650_2 $$2MeSH$$aHumans
000139632 650_2 $$2MeSH$$aLongevity
000139632 650_2 $$2MeSH$$aNeurodegenerative Diseases: metabolism
000139632 650_2 $$2MeSH$$aPoly(A)-Binding Protein I: metabolism
000139632 650_2 $$2MeSH$$aPrions: metabolism
000139632 650_2 $$2MeSH$$aProtein Aggregation, Pathological: metabolism
000139632 650_2 $$2MeSH$$aProteome: chemistry
000139632 650_2 $$2MeSH$$aRNA: metabolism
000139632 650_2 $$2MeSH$$aRNA-Binding Proteins: metabolism
000139632 650_2 $$2MeSH$$aStress, Physiological
000139632 650_2 $$2MeSH$$aTranscription Factors: metabolism
000139632 7001_ $$0P:(DE-2719)2810353$$aDavid, Della C$$b1$$eLast author$$udzne
000139632 77318 $$2Crossref$$3journal-article$$a10.1080/19336896.2017.1356559$$b : Informa UK Limited, 2017-09-03$$n5$$p313-322$$tPrion$$v11$$x1933-6896$$y2017
000139632 773__ $$0PERI:(DE-600)2267671-5$$a10.1080/19336896.2017.1356559$$gVol. 11, no. 5, p. 313 - 322$$n5$$p313-322$$q11:5<313 - 322$$tPrion$$v11$$x1933-6896$$y2017
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