Evidence map›Paper›PMID 29523690›Full record

ArticleThe Journal of biological chemistry2018

Cross-talk between chromatin acetylation and SUMOylation of tripartite motif-containing protein 24 (TRIM24) impacts cell adhesion.

Srikanth Appikonda, Kaushik N Thakkar, Parantu K Shah, Sharon Y R Dent, Jannik N Andersen, Michelle C Barton

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Review
  3. High-Affinity Peptide-Drug Conjugate Ligands for the TRIM24 PHD and Bromodomain.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
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  7. Insights into the protein domains of C-VI TRIM subfamily in viral infection.Frontiers in cellular and infection microbiology · 2025
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Srikanth AppikondaDepartment of Epigenetics and Molecular Carcinogenesis, Center for Cancer Epigenetics, Houston, Texas 77030.
Kaushik N ThakkarDepartment of Epigenetics and Molecular Carcinogenesis, Center for Cancer Epigenetics, Houston, Texas 77030; University of Texas M.D. Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences at Houston, Houston, Texas 77030.
Parantu K ShahInstitute for Applied Cancer Science, University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030.
Sharon Y R DentDepartment of Epigenetics and Molecular Carcinogenesis, Center for Cancer Epigenetics, Houston, Texas 77030; University of Texas M.D. Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences at Houston, Houston, Texas 77030.
Jannik N AndersenInstitute for Applied Cancer Science, University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030.
Michelle C BartonDepartment of Epigenetics and Molecular Carcinogenesis, Center for Cancer Epigenetics, Houston, Texas 77030; University of Texas M.D. Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences at Houston, Houston, Texas 77030. Electronic address: mbarton@mdanderson.org.
The University of Texas MD Anderson Cancer Center · US

Funding

Tumor Evolution and Metastasis ProgramP30CA016672 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Scott Kopetz · 1985 to 2026
$290.8M
NCI NIH HHS P30 CA016672
6 · The paper itself

Abstract

Proteins with domains that recognize and bind post-translational modifications (PTMs) of histones are collectively termed epigenetic readers. Numerous interactions between specific reader protein domains and histone PTMs and their regulatory outcomes have been reported, but little is known about how reader proteins may in turn be modulated by these interactions. Tripartite motif-containing protein 24 (TRIM24) is a histone reader aberrantly expressed in multiple cancers. Here, our investigation revealed functional cross-talk between histone acetylation and TRIM24 SUMOylation. Binding of TRIM24 to chromatin via its tandem PHD-bromodomain, which recognizes unmethylated lysine 4 and acetylated lysine 23 of histone H3 (H3K4me0/K23ac), led to TRIM24 SUMOylation at lysine residues 723 and 741. Inactivation of the bromodomain, either by mutation or with a small-molecule inhibitor, IACS-9571, abolished TRIM24 SUMOylation. Conversely, inhibition of histone deacetylation markedly increased TRIM24's interaction with chromatin and its SUMOylation. Of note, gene expression profiling of MCF7 cells expressing WT

Indexed as

Cell AdhesionSumoylationAcetylationCarrier ProteinsChromatinEpigenesis, GeneticHEK293 CellsHistonesHumansMCF-7 CellsOncogenesProtein Processing, Post-TranslationalCarrier ProteinsChromatinHistonesTRIM24 protein, humanbreast cancerbromodomaincell adhesionchromatin modificationepigeneticshistone acetylationhistone readerreader proteinSUMOylationTRIM24

Identifiers

PMID29523690
PMCPMC5950014
OpenAlexW2789822585

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.