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http://purl.uniprot.org/citations/32399915http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32399915http://www.w3.org/2000/01/rdf-schema#comment"HIF-1-mediated adaptation to changes in oxygen availability is a critical aspect of healthy physiology. HIF is regulated by a conserved mechanism whereby EGLN/PHD family members hydroxylate HIF in an oxygen-dependent manner, targeting it for ubiquitination by Von-Hippel-Lindau (VHL) family members, leading to its proteasomal degradation. The activity of the only C. elegans PHD family member, EGL-9, is also regulated by a hydrogen sulfide sensing cysteine-synthetase-like protein, CYSL-1, which is, in turn, regulated by RHY-1/acyltransferase. Over the last decade, multiple seminal studies have established a role for the hypoxic response in regulating longevity, with mutations in vhl-1 substantially extending C. elegans lifespan through a HIF-1-dependent mechanism. However, studies on other components of the hypoxic signaling pathway that similarly stabilize HIF-1 have shown more mixed results, suggesting that mutations in egl-9 and rhy-1 frequently fail to extend lifespan. Here, we show that egl-9 and rhy-1 mutants suppress the long-lived phenotype of vhl-1 mutants. We also show that RNAi of rhy-1 extends lifespan of wild-type worms while decreasing lifespan of vhl-1 mutant worms. We further identify VHL-1-independent gene expression changes mediated by EGL-9 and RHY-1 and find that a subset of these genes contributes to longevity regulation. The resulting data suggest that changes in HIF-1 activity derived by interactions with EGL-9 likely contribute greatly to its role in regulation of longevity."xsd:string
http://purl.uniprot.org/citations/32399915http://purl.org/dc/terms/identifier"doi:10.1007/s11357-020-00194-0"xsd:string
http://purl.uniprot.org/citations/32399915http://purl.uniprot.org/core/author"Huang S."xsd:string
http://purl.uniprot.org/citations/32399915http://purl.uniprot.org/core/author"Leiser S.F."xsd:string
http://purl.uniprot.org/citations/32399915http://purl.uniprot.org/core/author"Sarker M."xsd:string
http://purl.uniprot.org/citations/32399915http://purl.uniprot.org/core/author"Miller H.A."xsd:string
http://purl.uniprot.org/citations/32399915http://purl.uniprot.org/core/author"Fretz A."xsd:string
http://purl.uniprot.org/citations/32399915http://purl.uniprot.org/core/author"Howington M."xsd:string
http://purl.uniprot.org/citations/32399915http://purl.uniprot.org/core/author"Kruempel J.C.P."xsd:string
http://purl.uniprot.org/citations/32399915http://purl.uniprot.org/core/author"Schaller M.L."xsd:string
http://purl.uniprot.org/citations/32399915http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32399915http://purl.uniprot.org/core/name"Geroscience"xsd:string
http://purl.uniprot.org/citations/32399915http://purl.uniprot.org/core/pages"1621-1633"xsd:string
http://purl.uniprot.org/citations/32399915http://purl.uniprot.org/core/title"Hypoxic response regulators RHY-1 and EGL-9/PHD promote longevity through a VHL-1-independent transcriptional response."xsd:string
http://purl.uniprot.org/citations/32399915http://purl.uniprot.org/core/volume"42"xsd:string
http://purl.uniprot.org/citations/32399915http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/32399915
http://purl.uniprot.org/citations/32399915http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/32399915
http://purl.uniprot.org/uniprot/#_G5EBV0-mappedCitation-32399915http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32399915
http://purl.uniprot.org/uniprot/#_Q19213-mappedCitation-32399915http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32399915
http://purl.uniprot.org/uniprot/#_Q9XVW1-mappedCitation-32399915http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32399915
http://purl.uniprot.org/uniprot/Q19213http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32399915
http://purl.uniprot.org/uniprot/G5EBV0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32399915
http://purl.uniprot.org/uniprot/Q9XVW1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32399915