Evidence map›Paper›PMID 23027873›Full record

ArticleThe Journal of biological chemistry2012

Cross-talk among RNA polymerase II kinases modulates C-terminal domain phosphorylation.

Ballachanda N Devaiah, Dinah S Singer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed, 61 citations in OpenAlex.

  1. Trial
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  11. Innate Immunity, Epithelial Plasticity, and Remodeling in Asthma.Advances in experimental medicine and biology · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. The emerging role of BET inhibitors in breast cancer.Breast (Edinburgh, Scotland) · 2020
    Review
  19. Article
  20. MYC protein stability is negatively regulated by BRD4.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Ballachanda N DevaiahExperimental Immunology Branch, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA.
Dinah S Singer
National Institutes of Health · US

Funding

Brd4 is an atypical kinase that regulates transcriptionZIABC011381 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SINGER, DINAH S. · 2011 to 2025
$5.4M
Intramural NIH HHS
6 · The paper itself

Abstract

The RNA polymerase II (Pol II) C-terminal domain (CTD) serves as a docking site for numerous proteins, bridging various nuclear processes to transcription. The recruitment of these proteins is mediated by CTD phospho-epitopes generated during transcription. The mechanisms regulating the kinases that establish these phosphorylation patterns on the CTD are not known. We report that three CTD kinases, CDK7, CDK9, and BRD4, engage in cross-talk, modulating their subsequent CTD phosphorylation. BRD4 phosphorylates PTEFb/CDK9 at either Thr-29 or Thr-186, depending on its relative abundance, which represses or activates CDK9 CTD kinase activity, respectively. Conversely, CDK9 phosphorylates BRD4 enhancing its CTD kinase activity. The CTD Ser-5 kinase CDK7 also interacts with and phosphorylates BRD4, potently inhibiting BRD4 kinase activity. Additionally, the three kinases regulate each other indirectly through the general transcription factor TAF7. An inhibitor of CDK9 and CDK7 CTD kinase activities, TAF7 also binds to BRD4 and inhibits its kinase activity. Each of these kinases phosphorylates TAF7, affecting its subsequent ability to inhibit the other two. Thus, a complex regulatory network governs Pol II CTD kinases.

Indexed as

AnimalsBromodomain Containing ProteinsCell Cycle ProteinsCell LineCyclin-Dependent Kinase 9Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesDNA DamageDrosophilaHeLa CellsHumansModels, BiologicalNuclear ProteinsPhosphorylationProtein Structure, TertiaryRNA Polymerase IIBRD4 protein, humanBromodomain Containing ProteinsCDK9 protein, humanCell Cycle ProteinsCyclin-Dependent Kinase 9Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesNuclear ProteinsRNA Polymerase IISerineTAF7 protein, humanTATA-Binding Protein Associated FactorsTranscription FactorsTranscription Factor TFIID

Identifiers

PMID23027873
PMCPMC3493918
OpenAlexW1988708761

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.