Evidence map›Paper›PMID 30377265›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

KDM3A histone demethylase functions as an essential factor for activation of JAK2-STAT3 signaling pathway.

Hyunkyung Kim, Dongha Kim, Seon Ah Choi, Chang Rok Kim, Se Kyu Oh, Ki Eun Pyo, Joomyung Kim, Seung-Hoon Lee, Jong-Bok Yoon, Yi Zhang and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

29 citing papers in PubMed, 55 citations in OpenAlex.

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  17. JMJD family proteins in cancer and inflammation.Signal transduction and targeted therapy · 2022
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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

11 authors at 3 institutions in 2 countries.

Hyunkyung KimCreative Research Initiatives Center for Epigenetic Code and Diseases, Department of Biological Sciences, Seoul National University, 08826 Seoul, South Korea.
Dongha KimCreative Research Initiatives Center for Epigenetic Code and Diseases, Department of Biological Sciences, Seoul National University, 08826 Seoul, South Korea.
Seon Ah ChoiCreative Research Initiatives Center for Epigenetic Code and Diseases, Department of Biological Sciences, Seoul National University, 08826 Seoul, South Korea.
Chang Rok KimCreative Research Initiatives Center for Epigenetic Code and Diseases, Department of Biological Sciences, Seoul National University, 08826 Seoul, South Korea.
Se Kyu OhCreative Research Initiatives Center for Epigenetic Code and Diseases, Department of Biological Sciences, Seoul National University, 08826 Seoul, South Korea.
Ki Eun PyoCreative Research Initiatives Center for Epigenetic Code and Diseases, Department of Biological Sciences, Seoul National University, 08826 Seoul, South Korea.
Joomyung KimCreative Research Initiatives Center for Epigenetic Code and Diseases, Department of Biological Sciences, Seoul National University, 08826 Seoul, South Korea.
Seung-Hoon LeeDepartment of Biochemistry, Translational Research Center for Protein Function Control, Yonsei University, 03722 Seoul, South Korea.
Jong-Bok YoonDepartment of Biochemistry, Translational Research Center for Protein Function Control, Yonsei University, 03722 Seoul, South Korea.
Yi ZhangHoward Hughes Medical Institute, Harvard Medical School, Boston, MA 02115.
Sung Hee BaekCreative Research Initiatives Center for Epigenetic Code and Diseases, Department of Biological Sciences, Seoul National University, 08826 Seoul, South Korea; sbaek@snu.ac.kr.
Seoul National University · KRYonsei University · KRHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Janus tyrosine kinase 2 (JAK2)-signal transducer and activator of transcription 3 (STAT3) signaling pathway is essential for modulating cellular development, differentiation, and homeostasis. Thus, dysregulation of JAK2-STAT3 signaling pathway is frequently associated with human malignancies. Here, we provide evidence that lysine-specific demethylase 3A (KDM3A) functions as an essential epigenetic enzyme for the activation of JAK2-STAT3 signaling pathway. KDM3A is tyrosine-phosphorylated by JAK2 in the nucleus and functions as a STAT3-dependent transcriptional coactivator. JAK2-KDM3A signaling cascade induced by IL-6 leads to alteration of histone H3K9 methylation as a predominant epigenetic event, thereby providing the functional and mechanistic link between activation of JAK2-STAT3 signaling pathway and its epigenetic control. Together, our findings demonstrate that inhibition of KDM3A phosphorylation could be a potent therapeutic strategy to control oncogenic effect of JAK2-STAT3 signaling pathway.

Indexed as

Epigenesis, GeneticHEK293 CellsHeLa CellsHistonesHumansInterleukin-6Janus Kinase 2Jumonji Domain-Containing Histone DemethylasesPhosphorylationProtein-Tyrosine KinasesSignal TransductionSTAT3 Transcription FactorTranscriptional ActivationHistonesInterleukin-6JAK2 protein, humanJanus Kinase 2Jumonji Domain-Containing Histone DemethylasesKDM3A protein, humanProtein-Tyrosine KinasesSTAT3 protein, humanSTAT3 Transcription Factorhistone demethylationJAK2KDM3AphosphorylationSTAT3

Identifiers

PMID30377265
PMCPMC6243239
OpenAlexW2898985668

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.