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http://purl.uniprot.org/citations/17317627http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17317627http://www.w3.org/2000/01/rdf-schema#comment"The RNA binding protein HuR regulates the stability of many target mRNAs. Here, we report that HuR associated with the 3' untranslated region of the mRNA encoding the longevity and stress-response protein SIRT1, stabilized the SIRT1 mRNA, and increased SIRT1 expression levels. Unexpectedly, oxidative stress triggered the dissociation of the [HuR-SIRT1 mRNA] complex, in turn promoting SIRT1 mRNA decay, reducing SIRT1 abundance, and lowering cell survival. The cell cycle checkpoint kinase Chk2 was activated by H(2)O(2), interacted with HuR, and was predicted to phosphorylate HuR at residues S88, S100, and T118. Mutation of these residues revealed a complex pattern of HuR binding, with S100 appearing to be important for [HuR-SIRT1 mRNA] dissociation after H(2)O(2). Our findings demonstrate that HuR regulates SIRT1 expression, underscore functional links between the two stress-response proteins, and implicate Chk2 in these processes."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2007.01.011"xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/author"Gillespie D.A."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/author"Yang X."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/author"Walker M."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/author"Galban S."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/author"Lal A."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/author"Blethrow J.D."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/author"Kim H.H."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/author"Gorospe M."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/author"Abdelmohsen K."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/author"Furneaux H."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/author"Pullmann R. Jr."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/author"Shubert J."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/name"Mol Cell"xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/pages"543-557"xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/title"Phosphorylation of HuR by Chk2 regulates SIRT1 expression."xsd:string
http://purl.uniprot.org/citations/17317627http://purl.uniprot.org/core/volume"25"xsd:string
http://purl.uniprot.org/citations/17317627http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17317627
http://purl.uniprot.org/citations/17317627http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17317627
http://purl.uniprot.org/uniprot/Q96EB6#attribution-4C1A636270ADA8009AB10BEF534C3820http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/17317627
http://purl.uniprot.org/uniprot/#_E9PC49-mappedCitation-17317627http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17317627
http://purl.uniprot.org/uniprot/#_A8K128-mappedCitation-17317627http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17317627