Evidence map›Paper›PMID 19095693›Full record

ArticleNucleic acids research2009

A feedback regulatory loop between methyltransferase PRMT1 and orphan receptor TR3.

Na-zi Lei, Xiao-yan Zhang, Hang-zi Chen, Yuan Wang, Yan-yan Zhan, Zhong-hui Zheng, Yue-mao Shen, Qiao Wu

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

  1. LC-MS profiling ofbioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Article
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  9. Structure, Activity, and Function of PRMT1.Life (Basel, Switzerland) · 2021
    Review
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  12. Article
  13. Review
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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

8 authors at 1 institution in 1 country.

Na-zi LeiKey Laboratory of the Ministry of Education for Cell Biology and Tumor Cell Engineering, School of Life Sciences, Xiamen University, Xiamen 361005, Fujian Province, China.
Xiao-yan Zhang
Hang-zi Chen
Yuan Wang
Yan-yan Zhan
Zhong-hui Zheng
Yue-mao Shen
Qiao Wu
Xiamen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PRMT1, an arginine methyltransferase, plays an important role in numerous cellular processes. In this study, we demonstrate a feedback regulatory loop between PRMT1 and the orphan receptor TR3. Unlike another orphan receptor HNF4, TR3 is not methylated by PRMT1 although they physically interact with each other. By delaying the TR3 protein degradation, PRMT1 binding leads to the elevation of TR3 cellular protein level, thereby enhances the DNA binding and transactivation activity of TR3 in a non-methyltransferase manner. Another coactivator SRC-2 acts synergistically with PRMT1 to regulate TR3 functions. In turn, TR3 binding to the catalytic domain of PRMT1 causes an inhibition of the PRMT1 methyltransferase activity. This repression results in the functional changes in some of PRMT1 substrates, including STAT3 and Sam68. The negative regulation of PRMT1 by TR3 was further confirmed in both TR3-knockdown cells and TR3-knockout mice with the use of an agonist for TR3. Taken together, our study not only identifies a regulatory role of PRMT1, independent on methyltransferase activity, in TR3 transactivation, but also characterizes a novel function of TR3 in the repression of PRMT1 methyltransferase activity.

Indexed as

Feedback, PhysiologicalAnimalsCell LineDNA-Binding ProteinsHumansMiceMice, KnockoutNuclear Receptor Coactivator 2Nuclear Receptor Subfamily 4, Group A, Member 1Protein-Arginine N-MethyltransferasesReceptors, SteroidRepressor ProteinsDNA-Binding ProteinsNR4A1 protein, humanNr4a1 protein, mouseNuclear Receptor Coactivator 2Nuclear Receptor Subfamily 4, Group A, Member 1PRMT1 protein, humanProtein-Arginine N-MethyltransferasesReceptors, SteroidRepressor Proteins

Identifiers

PMID19095693
PMCPMC2647306
OpenAlexW2010626418

What OpenQuestion holds

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LicenceCC BY-NC
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.