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http://purl.uniprot.org/citations/37099597http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37099597http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37099597http://www.w3.org/2000/01/rdf-schema#comment"Oxidative stress response is a fundamental biological process mediated by conserved mechanisms. The identities and functions of some key regulators remain unknown. Here, we report a novel role of C. elegans casein kinase 1 gamma CSNK-1 (also known as CK1γ or CSNK1G) in regulating oxidative stress response and ROS levels. csnk-1 interacted with the bli-3/tsp-15/doxa-1 NADPH dual oxidase genes via genetic nonallelic noncomplementation to affect C. elegans survival in oxidative stress. The genetic interaction was supported by specific biochemical interactions between DOXA-1 and CSNK-1 and potentially between their human orthologs DUOXA2 and CSNK1G2. Consistently, CSNK-1 was required for normal ROS levels in C. elegans. CSNK1G2 and DUOXA2 each can promote ROS levels in human cells, effects that were suppressed by a small molecule casein kinase 1 inhibitor. We also detected genetic interactions between csnk-1 and skn-1 Nrf2 in oxidative stress response. Together, we propose that CSNK-1 CSNK1G defines a novel conserved regulatory mechanism for ROS homeostasis."xsd:string
http://purl.uniprot.org/citations/37099597http://purl.org/dc/terms/identifier"doi:10.1371/journal.pgen.1010740"xsd:string
http://purl.uniprot.org/citations/37099597http://purl.org/dc/terms/identifier"doi:10.1371/journal.pgen.1010740"xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/author"Hu Y."xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/author"Hu Y."xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/author"Ma L."xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/author"Ma L."xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/author"Xu Z."xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/author"Xu Z."xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/author"Pan Q."xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/author"Pan Q."xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/name"PLoS Genet."xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/name"PLoS Genet."xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/pages"e1010740"xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/pages"e1010740"xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/title"Casein kinase 1 gamma regulates oxidative stress response via interacting with the NADPH dual oxidase complex."xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/title"Casein kinase 1 gamma regulates oxidative stress response via interacting with the NADPH dual oxidase complex."xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/37099597http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/37099597http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/37099597
http://purl.uniprot.org/citations/37099597http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/37099597