Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation.

Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation. Research Abstract Details 

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Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation. Abstract Text:

Eric Metzger,Na Yin,Melanie Wissmann,Natalia Kunowska,Kristin Fischer,Nicolaus Friedrichs,Debasis Patnaik,Jonathan M G Higgins,Noelle Potier,Karl-Heinz Scheidtmann,Reinhard Buettner,Roland ,Eric Metzger,Na Yin,Melanie Wissmann,Natalia Kunowska,Kristin Fischer,Nicolaus Friedrichs,Debasis Patnaik,Jonathan M G Higgins,Noelle Potier,Karl-Heinz Scheidtmann,Reinhard Buettner,Roland ,Eric Metzger,Na Yin,Melanie Wissmann,Natalia Kunowska,Kristin Fischer,Nicolaus Friedrichs,Debasis Patnaik,Jonathan M G Higgins,Noelle Potier,Karl-Heinz Scheidtmann,Reinhard Buettner,Roland ,

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.

Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation. Publishing Authors By Initials

E Metzger,N Yin,M Wissmann,N Kunowska,K Fischer,N Friedrichs,D Patnaik,JM Higgins,N Potier,KH Scheidtmann,R Buettner,R ,E Metzger,N Yin,M Wissmann,N Kunowska,K Fischer,N Friedrichs,D Patnaik,JM Higgins,N Potier,KH Scheidtmann,R Buettner,R ,E Metzger,N Yin,M Wissmann,N Kunowska,K Fischer,N Friedrichs,D Patnaik,JM Higgins,N Potier,KH Scheidtmann,R Buettner,R ,

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Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Nature cell biology

VOLUME: 10

Page Numbers: 53-60

Journal Abbreviation: Nat. Cell Biol.

ISSN: 1465-7392

DAY: 9

MONTH: 12

YEAR: 2007

Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation. Information

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LANGUAGE: eng

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Grant and Affiliation Information for Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation.

AFFILIATION: Universitäts-Frauenklinik und Zentrale Klinische Forschung, Klinikum der Universität Freiburg, Breisacherstrasse 66, 79106 Freiburg, Germany.

Country: England

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MEDLINETA: Nat Cell Biol

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