Evidence map›Paper›PMID 38773077›Full record

ArticleCell death discovery2024

TAF2, within the TFIID complex, regulates the expression of a subset of protein-coding genes.

I-Hsin Cheng, Wen-Chieh Pi, Chung-Hao Hsu, Yiran Guo, Jun-Lin Lai, Gang G Wang, Bon-Chu Chung, Robert G Roeder, Wei-Yi Chen

Abstract read
In one paragraph

Article in Cell death discovery, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

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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

4 citing papers in PubMed.

  1. The molecular basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  3. A recently evolved TAF8 isoform arising from anbioRxiv : the preprint server for biology · 2026
    Article
  4. 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

9 authors.

I-Hsin ChengInstitute of Biochemistry and Molecular Biology, National Yang Ming Chiao Tung University, Taipei, Taiwan.
Wen-Chieh PiInstitute of Biochemistry and Molecular Biology, National Yang Ming Chiao Tung University, Taipei, Taiwan.ORCID http://orcid.org/0000-0002-9777-1455
Chung-Hao HsuSchool of Medicine, College of Medicine, National Yang Ming Chiao Tung University, Taipei, Taiwan.
Yiran GuoDepartment of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, NC, 27710, USA.
Jun-Lin LaiProgram in Molecular Medicine, National Yang Ming Chiao Tung University and Academia Sinica, Taipei, Taiwan.
Gang G WangDepartment of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, NC, 27710, USA.ORCID http://orcid.org/0000-0002-7210-9940
Bon-Chu ChungInsitute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Robert G RoederLaboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, NY, 10065, USA.
Wei-Yi ChenInstitute of Biochemistry and Molecular Biology, National Yang Ming Chiao Tung University, Taipei, Taiwan. chenwy@nycu.edu.tw.ORCID http://orcid.org/0000-0002-0661-6899

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TFIID, one of the general transcription factor (GTF), regulates transcriptional initiation of protein-coding genes through direct binding to promoter elements and subsequent recruitment of other GTFs and RNA polymerase II. Although generally required for most protein-coding genes, accumulated studies have also demonstrated promoter-specific functions for several TFIID subunits in gene activation. Here, we report that TBP-associated factor 2 (TAF2) specifically regulates TFIID binding to a small subset of protein-coding genes and is essential for cell growth of multiple cancer lines. Co-immunoprecipitation assays revealed that TAF2 may be sub-stoichiometrically associated with the TFIID complex, thus indicating a minor fraction of TAF2-containing TFIID in cells. Consistently, integrated genome-wide profiles show that TAF2 binds to and regulates only a small subset of protein-coding genes. Furthermore, through the use of an inducible TAF2 degradation system, our results reveal a reduction of TBP/TFIID binding to several ribosomal genes upon selective ablation of TAF2. In addition, depletion of TAF2, as well as the TAF2-regulated ribosomal protein genes RPL30 and RPL39, decreases ribosome assembly and global protein translation. Collectively, this study suggests that TAF2 within the TFIID complex is of functional importance for TBP/TFIID binding to and expression of a small subset of protein-coding genes, thus establishing a previously unappreciated promoter-selective function for TAF2.

Identifiers

PMID38773077
PMCPMC11109217

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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.