ArticleMolecular and cellular biology1999
hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 82 citations in OpenAlex.
- Splicing as an integrative layer linking cell cycle regulation, epigenetic dynamics, and environmental responses in plants.Frontiers in plant science · 2026Review
- Role of the SAF-A/HNRNPU SAP domain in X chromosome inactivation, nuclear dynamics, transcription, splicing, and cell proliferation.PLoS genetics · 2025Article
- Regulation of HNRNP family by post-translational modifications in cancer.Cell death discovery · 2024Review
- m6A-dependent mature miR-151-5p accelerates the malignant process of HNSCC by targeting LYPD3.Molecular biomedicine · 2024Article
- N-terminal tagging of RNA Polymerase II shapes transcriptomes more than C-terminal alterations.iScience · 2024Article
- Biological functions and clinic significance of SAF‑A (Review).Biomedical reports · 2024Review
- Evidence of shared transcriptomic dysregulation of HNRNPU-related disorder between human organoids and embryonic mice.iScience · 2023Article
- SAF-A/hnRNP U binds polyphosphoinositides via a lysine rich polybasic motif located in the SAP domain.microPublication biology · 2023Article
- [Clinical significance and pathogenesis analysis of heterogeneous nuclear ribonucleoprotein U in acute myeloid leukemia].Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi · 2022Article
- SAF-A mutants disrupt chromatin structure through dominant negative effects on RNAs associated with chromatin.Mammalian genome : official journal of the International Mammalian Genome Society · 2022Article
- A Monoclonal Anti-HMGB1 Antibody Attenuates Neurodegeneration in an Experimental Animal Model of Glaucoma.International journal of molecular sciences · 2022Article
- Epigenetic Regulation of Cellular Senescence.Cells · 2022Review
- Gene Architecture Facilitates Intron-Mediated Enhancement of Transcription.Frontiers in molecular biosciences · 2021Review
- hnRNPU in Sertoli cells cooperates with WT1 and is essential for testicular development by modulating transcriptional factorsTheranostics · 2021Article
- Novel Cell-Penetrating Peptides Derived From Scaffold-Attachment- Factor A Inhibits Cancer Cell Proliferation and Survival.Frontiers in oncology · 2021Article
- Novel Non-Coding Transcript inFrontiers in oncology · 2020Article
- Article
- The hnRNP RALY regulates transcription and cell proliferation by modulating the expression of specific factors including the proliferation marker E2F1.The Journal of biological chemistry · 2017Article
- Xist Exon 7 Contributes to the Stable Localization of Xist RNA on the Inactive X-Chromosome.PLoS genetics · 2015Article
- hnRNP U enhances caspase-9 splicing and is modulated by AKT-dependent phosphorylation of hnRNP L.The Journal of biological chemistry · 2013Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This study describes a potential new function of hnRNP U as an RNA polymerase (Pol II) elongation inhibitor. We demonstrated that a subfraction of human hnRNP U is associated with the Pol II holoenzyme in vivo and as such recruited to the promoter as part of the preinitiation complex. hnRNP U, however, appears to dissociate from the Pol II complex at the early stage of transcription and is therefore absent from the elongating Pol II complex. When tested in the human immunodeficiency virus type 1 transcription system, hnRNP U inhibits elongation rather than initiation of transcription by Pol II. This inhibition requires the carboxy-terminal domain (CTD) of Pol II. We showed that hnRNP U can bind TFIIH in vivo under certain conditions and inhibit TFIIH-mediated CTD phosphorylation in vitro. We find that the middle domain of hnRNP U is sufficient to mediate its Pol II association and its inhibition of TFIIH-mediated phosphorylation and Pol II elongation. The abilities of hnRNP U to inhibit TFIIH-mediated CTD phosphorylation and its Pol II association are necessary for hnRNP U to mediate the repression of Pol II elongation. Based on these observations, we suggest that a subfraction of hnRNP U, as a component of the Pol II holoenzyme, may downregulate TFIIH-mediated CTD phosphorylation in the basal transcription machinery and repress Pol II elongation. With such functions, hnRNP U might provide one of the mechanisms by which the CTD is maintained in an unphosphorylated state in the Pol II holoenzyme.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.