Evidence map›Paper›PMID 12138181›Full record

ArticleMolecular and cellular biology2002

Involvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor.

Jiwen Li, Qiushi Lin, Ho-Geun Yoon, Zhi-Qing Huang, Brian D Strahl, C David Allis, Jiemin Wong

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

59 citing papers in PubMed, 139 citations in OpenAlex.

  1. Article
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  3. Thyroid hormone links environmental signals to DNA methylation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
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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

7 authors at 2 institutions in 1 country.

Jiwen LiDepartment of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030, USA.
Qiushi Lin
Ho-Geun Yoon
Zhi-Qing Huang
Brian D Strahl
C David Allis
Jiemin Wong
Baylor College of Medicine · USUniversity of Virginia Health System · US

Funding

INFLUENCE OF HISTONE H1 AND HMGS ON GENE EXPRESSIONR01GM040922 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI ALLIS, CHARLES DAVID · 1989 to 2022
$10.0M
CHARACTERIZATION OF COREPRESSOR N-COR COMPLEXESR01DK058679 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI WONG, JIEMIN · 2001 to 2005
$1.2M
THYROID HORMONE RECEPTOR ACTION IN CHROMATINR01DK056324 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI WONG, JIEMIN · 1999 to 2003
$947k
NIDDK NIH HHS DK56324NIDDK NIH HHS DK58679NIDDK NIH HHS R01 DK056324NIDDK NIH HHS R01 DK058679NIGMS NIH HHS GM40922NIGMS NIH HHS R01 GM040922
6 · The paper itself

Abstract

Previous studies have established an important role of histone acetylation in transcriptional control by nuclear hormone receptors. With chromatin immunoprecipitation assays, we have now investigated whether histone methylation and phosphorylation are also involved in transcriptional regulation by thyroid hormone receptor (TR). We found that repression by unliganded TR is associated with a substantial increase in methylation of H3 lysine 9 (H3-K9) and a decrease in methylation of H3 lysine 4 (H3-K4), methylation of H3 arginine 17 (H3-R17), and a dual modification of phosphorylation of H3 serine 10 and acetylation of lysine 14 (pS10/acK14). On the other hand, transcriptional activation by liganded TR is coupled with a substantial decrease in both H3-K4 and H3-K9 methylation and a robust increase in H3-R17 methylation and the dual modification of pS10/acK14. Trichostatin A treatment results in not only histone hyperacetylation but also an increase in methylation of H3-K4, increase in dual modification of pS10/acK14, and reduction in methylation of H3-K9, revealing an extensive interplay between histone acetylation, methylation, and phosphorylation. In an effort to understand the underlying mechanism for an increase in H3-K9 methylation during repression by unliganded TR, we demonstrated that TR interacts in vitro with an H3-K9-specific histone methyltransferase (HMT), SUV39H1. Functional analysis indicates that SUV39H1 can facilitate repression by unliganded TR and in so doing requires its HMT activity. Together, our data uncover a novel role of H3-K9 methylation in repression by unliganded TR and provide strong evidence for the involvement of multiple distinct histone covalent modifications (acetylation, methylation, and phosphorylation) in transcriptional control by nuclear hormone receptors.

Indexed as

Gene Expression RegulationHistone-Lysine N-MethyltransferaseTranscription, GeneticAnimalsCell FractionationGenes, ReporterHistone MethyltransferasesHistonesHumansHydroxamic AcidsMethylationMethyltransferasesOocytesPhosphorylationProtein MethyltransferasesProtein Synthesis InhibitorsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesHydroxamic AcidsMethyltransferasesProtein MethyltransferasesProtein Synthesis InhibitorsReceptors, Thyroid Hormonetrichostatin A

Identifiers

PMID12138181
PMCPMC133990
OpenAlexW2132849597

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.