RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/18066052http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18066052http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18066052http://www.w3.org/2000/01/rdf-schema#comment"Posttranslational modifications of histones such as methylation, acetylation and phosphorylation regulate chromatin structure and gene expression. Here we show that protein-kinase-C-related kinase 1 (PRK1) phosphorylates histone H3 at threonine 11 (H3T11) upon ligand-dependent recruitment to androgen receptor target genes. PRK1 is pivotal to androgen receptor function because PRK1 knockdown or inhibition impedes androgen receptor-dependent transcription. Blocking PRK1 function abrogates androgen-induced H3T11 phosphorylation and inhibits androgen-induced demethylation of histone H3. Moreover, serine-5-phosphorylated RNA polymerase II is no longer observed at androgen receptor target promoters. Phosphorylation of H3T11 by PRK1 accelerates demethylation by the Jumonji C (JmjC)-domain-containing protein JMJD2C. Thus, phosphorylation of H3T11 by PRK1 establishes a novel chromatin mark for gene activation, identifying PRK1 as a gatekeeper of androgen receptor-dependent transcription. Importantly, levels of PRK1 and phosphorylated H3T11 correlate with Gleason scores of prostate carcinomas. Finally, inhibition of PRK1 blocks proliferation of androgen receptor-induced tumour cell proliferation, making PRK1 a promising therapeutic target."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.org/dc/terms/identifier"doi:10.1038/ncb1668"xsd:string
http://purl.uniprot.org/citations/18066052http://purl.org/dc/terms/identifier"doi:10.1038/ncb1668"xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Fischer K."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Fischer K."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Yin N."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Yin N."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Scheidtmann K.H."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Scheidtmann K.H."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Metzger E."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Metzger E."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Buettner R."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Buettner R."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Potier N."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Potier N."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Schule R."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Schule R."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Patnaik D."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Patnaik D."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Higgins J.M."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Higgins J.M."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Friedrichs N."xsd:string
http://purl.uniprot.org/citations/18066052http://purl.uniprot.org/core/author"Friedrichs N."xsd:string