Evidence map›Paper›PMID 23151507›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

G9a functions as a molecular scaffold for assembly of transcriptional coactivators on a subset of glucocorticoid receptor target genes.

Danielle Bittencourt, Dai-Ying Wu, Kwang Won Jeong, Daniel S Gerke, Laurie Herviou, Irina Ianculescu, Rajas Chodankar, Kimberly D Siegmund, Michael R Stallcup

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

88 citing papers in PubMed, 140 citations in OpenAlex.

  1. Review
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  9. Discovery of the First-in-Class G9a/GLP PROTAC Degrader.Journal of medicinal chemistry · 2024
    Article
  10. Discovery of the First-in-class G9a/GLP PROTAC Degrader.bioRxiv : the preprint server for biology · 2024
    Article
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  12. Review
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  20. Review

28 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 2 countries.

Danielle BittencourtDepartment of Biochemistry and Molecular Biology, USC Norris Comprehensive Cancer Center, University of Southern California, Los Angeles, CA 90089, USA.
Dai-Ying Wu
Kwang Won Jeong
Daniel S Gerke
Laurie Herviou
Irina Ianculescu
Rajas Chodankar
Kimberly D Siegmund
Michael R Stallcup
University of Southern California · USGachon University · KR

Funding

USC/NORRIS COMPREHENSIVE CANCER CENTER (CORE) SUPPORTP30CA014089 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI Fumito Ito · 1985 to 2026
$181.4M
Protein methyltransferases as transcriptional coregulatorsR37DK055274 · NIDDK · UNIVERSITY OF SOUTHERN CALIFORNIA · PI STALLCUP, MICHAEL R · 2008 to 2017
$5.3M
Protein methyltransferases as transcription coactivatorsR01DK055274 · NIDDK · UNIVERSITY OF SOUTHERN CALIFORNIA · PI STALLCUP, MICHAEL R · 1999 to 2007
$3.4M
Training in Genetic, Molecular and Cellular BiologyT32GM067587 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI STALLCUP, MICHAEL R · 2003 to 2012
$1.8M
NCI NIH HHS P30 CA014089NCI NIH HHS P30 CA 014089-36NIDDK NIH HHS R01 DK055274NIDDK NIH HHS R37 DK055274NIGMS NIH HHS T32 GM067587
6 · The paper itself

Abstract

Histone H3 lysine-9 methyltransferase G9a/EHMT2/KMT1C is a key corepressor of gene expression. However, activation of a limited number of genes by G9a (independent of its catalytic activity) has also been observed, although the precise molecular mechanisms are unknown. By using RNAi in combination with gene expression microarray analysis, we found that G9a functions as a positive and a negative transcriptional coregulator for discrete subsets of genes that are regulated by the hormone-activated Glucocorticoid Receptor (GR). G9a was recruited to GR-binding sites (but not to the gene body) of its target genes and interacted with GR, suggesting recruitment of G9a by GR. In contrast to its corepressor function, positive regulation of gene expression by G9a involved G9a-mediated enhanced recruitment of coactivators CARM1 and p300 to GR target genes. Further supporting a role for G9a as a molecular scaffold for its coactivator function, the G9a-specific methyltransferase inhibitor UNC0646 did not affect G9a coactivator function but selectively decreased G9a corepressor function for endogenous target genes. Overall, G9a functioned as a coactivator for hormone-activated genes and as a corepressor in support of hormone-induced gene repression, suggesting that the positive or negative actions of G9a are determined by the gene-specific regulatory environment and chromatin architecture. These findings indicate distinct mechanisms of G9a coactivator vs. corepressor functions in transcriptional regulation and provide insight into the molecular mechanisms of G9a coactivator function. Our results also suggest a physiological role of G9a in fine tuning the set of genes that respond to glucocorticoids.

Indexed as

BiocatalysisGene Expression RegulationHistocompatibility AntigensHistone-Lysine N-MethyltransferaseHumansReceptors, GlucocorticoidTrans-ActivatorsTranscription, GeneticEHMT2 protein, humanHistocompatibility AntigensHistone-Lysine N-MethyltransferaseReceptors, GlucocorticoidTrans-Activators

Identifiers

PMID23151507
PMCPMC3511704
OpenAlexW2037024585

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.