{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ji C"],"funding":["Hermann und Lilly Schilling-Stiftung für Medizinische Forschung","Deutsche Forschungsgemeinschaft","Graduate School of Life Sciences, Julius-Maximilians-Universität Würzburg","Interdisziplinäres Zentrum für Klinische Forschung, Universitätsklinikum Würzburg"],"pagination":["e55432"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9442301"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(9)"],"pubmed_abstract":["The P-TEFb complex promotes transcription elongation by releasing paused RNA polymerase II. P-TEFb itself is known to be inactivated through binding to the non-coding RNA 7SK but there is only limited information about mechanisms regulating their association. Here, we show that cells deficient in the RNA-binding protein hnRNP R, a known 7SK interactor, exhibit increased transcription due to phosphorylation of RNA polymerase II. Intriguingly, loss of hnRNP R promotes the release of P-TEFb from 7SK, accompanied by enhanced hnRNP A1 binding to 7SK. Additionally, we found that hnRNP R interacts with BRD4, and that hnRNP R depletion increases BRD4 binding to the P-TEFb component CDK9. Finally, CDK9 is stabilized upon loss of hnRNP R and its association with Cyclin K is enhanced. Together, our r"],"journal":["EMBO reports"],"pubmed_title":["hnRNP R negatively regulates transcription by modulating the association of P-TEFb with 7SK and BRD4."],"pmcid":["PMC9442301"],"funding_grant_id":["Fi573/20‐1","Fi573/15‐2","SE697/5‐2","BR4910/1‐2","SE697/4‐2","BR4910/2‐2"],"pubmed_authors":["Fischer U","Ji C","Deng C","Sendtner M","Schneider C","Antor K","Bischler T","Briese M"],"additional_accession":[]},"is_claimable":false,"name":"hnRNP R negatively regulates transcription by modulating the association of P-TEFb with 7SK and BRD4.","description":"The P-TEFb complex promotes transcription elongation by releasing paused RNA polymerase II. P-TEFb itself is known to be inactivated through binding to the non-coding RNA 7SK but there is only limited information about mechanisms regulating their association. Here, we show that cells deficient in the RNA-binding protein hnRNP R, a known 7SK interactor, exhibit increased transcription due to phosphorylation of RNA polymerase II. Intriguingly, loss of hnRNP R promotes the release of P-TEFb from 7SK, accompanied by enhanced hnRNP A1 binding to 7SK. Additionally, we found that hnRNP R interacts with BRD4, and that hnRNP R depletion increases BRD4 binding to the P-TEFb component CDK9. Finally, CDK9 is stabilized upon loss of hnRNP R and its association with Cyclin K is enhanced. Together, our r","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2025-04-05T10:26:14.017Z","creation":"2025-02-19T03:58:16.346Z"},"accession":"S-EPMC9442301","cross_references":{"pubmed":["35856391"],"doi":["10.15252/embr.202255432"]}}