Evidence map›Paper›PMID 23873942›Full record

ArticleGenes & development2013

A TAF4 coactivator function for E proteins that involves enhanced TFIID binding.

Wei-Yi Chen, Jinsong Zhang, Huimin Geng, Zhimei Du, Tomoyoshi Nakadai, Robert G Roeder

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed, 42 citations in OpenAlex.

  1. The molecular basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2026
    Review
  2. Review
  3. Distal enhancers loop to proximal enhancers, not to promoters.Nature reviews. Molecular cell biology · 2025
    Article
  4. Article
  5. Article
  6. The Function of E2A in B-Cell Development.Advances in experimental medicine and biology · 2024
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Relationship between the structure and function of the transcriptional regulator E2A.Journal of biological research (Thessalonike, Greece) · 2021
    Review
  13. What do Transcription Factors Interact With?Journal of molecular biology · 2021
    Review
  14. Mediator subunit MED1 is required for E2A-PBX1-mediated oncogenic transcription and leukemic cell growth.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Review
  16. Review
  17. Article
  18. Article
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  20. Review
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

6 authors at 2 institutions in 1 country.

Wei-Yi ChenLaboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10065, USA.
Jinsong Zhang
Huimin Geng
Zhimei Du
Tomoyoshi Nakadai
Robert G Roeder
Rockefeller University · USUniversity of California, San Francisco · US

Funding

Mechanisms of p53 target gene activation in DNA damage responsesR01CA129325 · NCI · ROCKEFELLER UNIVERSITY · PI ROEDER, ROBERT G · 2007 to 2011
$4.0M
Function and targeting of a stable transcription factor complex in leukemiaR01CA163086 · NCI · ROCKEFELLER UNIVERSITY · PI ROEDER, ROBERT G · 2011 to 2022
$3.6M
Role of OCA-B in B cell differentiation and malignancyR01CA113872 · NCI · ROCKEFELLER UNIVERSITY · PI ROEDER, ROBERT G · 2005 to 2009
$2.6M
NCI NIH HHS CA113872NCI NIH HHS CA129325NCI NIH HHS CA163086NCI NIH HHS R01 CA113872NCI NIH HHS R01 CA129325NCI NIH HHS R01 CA163086
6 · The paper itself

Abstract

The multisubunit TFIID plays a direct role in transcription initiation by binding to core promoter elements and directing preinitiation complex assembly. Although TFIID may also function as a coactivator through direct interactions with promoter-bound activators, mechanistic aspects of this poorly defined function remain unclear. Here, biochemical studies show a direct TFIID-E-protein interaction that (1) is mediated through interaction of a novel E-protein activation domain (activation domain 3 [AD3]) with the TAF homology (TAFH) domain of TAF4, (2) is critical for activation of a natural target gene by an E protein, and (3) mechanistically acts by enhancing TFIID binding to the core promoter. Complementary assays establish a gene-specific role for the TAFH domain in TFIID recruitment and activation of a large subset of genes in vivo. These results firmly establish TAF4 as a bona fide E-protein coactivator as well as a mechanism involving facilitated TFIID binding through direct interaction with an E-protein activation domain.

Indexed as

Basic Helix-Loop-Helix ProteinsGene DeletionGene Expression RegulationHeLa CellsHumansPromoter Regions, GeneticProtein BindingProtein Structure, TertiaryTATA-Binding Protein Associated FactorsTranscription Factor TFIIDTranscriptomeBasic Helix-Loop-Helix ProteinsTAF4 protein, humanTATA-Binding Protein Associated FactorsTranscription Factor TFIIDE2AE proteinsHEBTAF4TAFHTFIIDtranscription coactivator

Identifiers

PMID23873942
PMCPMC3731548
OpenAlexW2152027165

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.