Evidence map›Paper›PMID 39250704›Full record

ArticleACS chemical biology2024

Functional Investigations of p53 Acetylation Enabled by Heterobifunctional Molecules.

Li-Yun Chen, Soumya Jyoti Singha Roy, Appaso M Jadhav, Wesley W Wang, Pei-Hsin Chen, Timothy Bishop, Michael A Erb, Christopher G Parker

Abstract readLetter
In one paragraph

Article in ACS chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Induced proximity-based therapeutic modalities.Nature reviews. Drug discovery · 2026
    Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Harnessing the TAF1 Acetyltransferase for Targeted Acetylation of the Tumor Suppressor p53.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    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

8 authors.

Li-Yun ChenDepartment of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States.
Soumya Jyoti Singha RoyDepartment of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States.ORCID 0000-0002-7999-4591
Appaso M JadhavDepartment of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States.
Wesley W WangDepartment of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States.ORCID 0000-0002-7514-539X
Pei-Hsin ChenDepartment of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States.ORCID 0000-0003-3872-1017
Timothy BishopDepartment of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States.ORCID 0000-0002-0321-7809
Michael A ErbDepartment of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States.ORCID 0000-0001-9993-3481
Christopher G ParkerDepartment of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States.ORCID 0000-0001-8509-9289

Funding

Cancer-specific dependencies within the NuRD chromatin remodeler complex: new targets and chemical toolsR01CA280720 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI Michael A Erb · 2024 to 2026
$1.7M
NCI NIH HHS R01 CA280720
6 · The paper itself

Abstract

Post-translational modifications (PTMs) dynamically regulate the critical stress response and tumor suppressive functions of p53. Among these, acetylation events mediated by multiple acetyltransferases lead to differential target gene activation and subsequent cell fate. However, our understanding of these events is incomplete due to, in part, the inability to selectively and dynamically control p53 acetylation. We recently developed a heterobifunctional small molecule system, AceTAG, to direct the acetyltransferase p300/CBP for targeted protein acetylation in cells. Here, we expand AceTAG to leverage the acetyltransferase PCAF/GCN5 and apply these tools to investigate the functional consequences of targeted p53 acetylation in human cancer cells. We demonstrate that the recruitment of p300/CBP or PCAF/GCN5 to p53 results in distinct acetylation events and differentiated transcriptional activities. Further, we show that chemically induced acetylation of multiple hotspot p53 mutants results in increased stabilization and enhancement of transcriptional activity. Collectively, these studies demonstrate the utility of AceTAG for functional investigations of protein acetylation.

Indexed as

p300-CBP Transcription FactorsProtein Processing, Post-TranslationalTumor Suppressor Protein p53AcetylationCell Line, TumorHumansp300-CBP-Associated Factorp300-CBP-Associated Factorp300-CBP Transcription FactorsTP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID39250704
PMCPMC11421428

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.