Evidence map›Paper›PMID 22713873›Full record

ArticleGenes & development2012

The histone H3 Lys 27 demethylase JMJD3 regulates gene expression by impacting transcriptional elongation.

Shuzhen Chen, Jian Ma, Feizhen Wu, Li-Jun Xiong, Honghui Ma, Wenqi Xu, Ruitu Lv, Xiaodong Li, Judit Villen, Steven P Gygi and 2 more

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing 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

107 citing papers in PubMed, 173 citations in OpenAlex.

  1. Article
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  14. Review
  15. JMJD family proteins in cancer and inflammation.Signal transduction and targeted therapy · 2022
    Review
  16. Emerging roles of JMJD3 in cancer.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2022
    Review
  17. Article
  18. TruncatedScience advances · 2022
    Article
  19. Article
  20. Diverse Epigenetic Regulations of Macrophages in Atherosclerosis.Frontiers in cardiovascular medicine · 2022
    Review

47 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

12 authors at 5 institutions in 2 countries.

Shuzhen ChenDivision of Newborn Medicine and Program in Epigenetics, Department of Medicine, Children's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
Jian Ma
Feizhen Wu
Li-Jun Xiong
Honghui Ma
Wenqi Xu
Ruitu Lv
Xiaodong Li
Judit Villen
Steven P Gygi
Xiaole Shirley Liu
Yang Shi
Fudan University · CNHarvard University · USBoston Children's Hospital · USDana-Farber Cancer Institute · USDana-Farber/Harvard Cancer Center · US

Funding

Investigation of an unconventional co-repressor complexR01GM071004 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI SHI, YANG · 2004 to 2012
$2.7M
Inferring Mammalian Transcriptional Regulatory Networks from EpigenomicsR01GM099409 · NIGMS · DANA-FARBER CANCER INST · PI LIU, XIAOLE SHIRLEY · 2011 to 2014
$1.4M
NIGMS NIH HHS GM071004NIGMS NIH HHS GM099409NIGMS NIH HHS R01 GM071004NIGMS NIH HHS R01 GM099409
6 · The paper itself

Abstract

The histone H3 Lys 27 (H3K27) demethylase JMJD3 has been shown to play important roles in transcriptional regulation and cell differentiation. However, the mechanism underlying JMJD3-mediated transcriptional regulation remains incompletely understood. Here we show that JMJD3 is associated with KIAA1718, whose substrates include dimethylated H3K27 (H3K27me2), and proteins involved in transcriptional elongation. JMJD3 and KIAA1718 directly bind to and regulate the expression of a plethora of common target genes in both a demethylase activity-dependent and -independent manner in the human promyelocytic leukemia cell line HL-60. We found that JMJD3 and KIAA1718 collaborate to demethylate trimethylated H3K27 (H3K27me3) on a subset of their target genes, some of which are bivalently marked by H3K4me3 and H3K27me3 and associated with promoter-proximal, paused RNA polymerase II (Pol II) before activation. Reduction of either JMJD3 or KIAA1718 diminishes Pol II traveling along the gene bodies of the affected genes while having no effect on the promoter-proximal Pol II. Furthermore, JMJD3 and KIAA1718 also play a role in localizing elongation factors SPT6 and SPT16 to the target genes. Our results support the model whereby JMJD3 activates bivalent gene transcription by demethylating H3K27me3 and promoting transcriptional elongation. Taken together, these findings provide new insight into the mechanisms by which JMJD3 regulates gene expression.

Indexed as

Gene Expression Regulation, NeoplasticTranscription, GeneticBinding SitesCell Cycle ProteinsCell DifferentiationHistonesHL-60 CellsHumansJumonji Domain-Containing Histone DemethylasesLysineMacrophagesMethylationModels, BiologicalPhenotypeRNA Polymerase IITetradecanoylphorbol AcetateCell Cycle ProteinsHistonesJumonji Domain-Containing Histone DemethylasesKDM6B protein, humanKDM7A protein, humanLysineRNA Polymerase IISUPT16H protein, humanSUPT6H protein, humanTetradecanoylphorbol AcetateTranscription Factors

Identifiers

PMID22713873
PMCPMC3387663
OpenAlexW2051553283

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.