Evidence map›Paper›PMID 20798359›Full record

ArticleCirculation research2010

Disruption of protein arginine N-methyltransferase 2 regulates leptin signaling and produces leanness in vivo through loss of STAT3 methylation.

Hiroaki Iwasaki, Jason C Kovacic, Michelle Olive, Jeanette K Beers, Takanobu Yoshimoto, Martin F Crook, Leonardo H Tonelli, Elizabeth G Nabel

Open access · bronzeAbstract read
In one paragraph

Article in Circulation research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

40 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
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  7. Lysine and arginine methylation of transcription factors.Cellular and molecular life sciences : CMLS · 2024
    Review
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  13. Protein arginine methylation in transcription and epigenetic regulation.Frontiers in epigenetics and epigenomics · 2023
    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.

Hiroaki IwasakiBrigham and Women's Hospital, 75 Francis St, PB408, Boston, MA 02115, USA.
Jason C Kovacic
Michelle Olive
Jeanette K Beers
Takanobu Yoshimoto
Martin F Crook
Leonardo H Tonelli
Elizabeth G Nabel
University of Maryland, Baltimore · US

Funding

Intramural NIH HHS
6 · The paper itself

Abstract

rationaleArginine methylation by protein N-arginine methyltransferases (PRMTs) is an important posttranslational modification in the regulation of protein signaling. PRMT2 contains a highly conserved catalytic Ado-Met binding domain, but the enzymatic function of PRMT2 with respect to methylation is unknown. The JAK-STAT pathway is proposed to be regulated through direct arginine methylation of STAT transcription factors, and STAT3 signaling is known to be required for leptin regulation of energy balance.

objectiveTo identify the potential role of STAT3 arginine methylation by PRMT2 in the regulation of leptin signaling and energy homeostasis. METHODS AND

resultsWe identified that PRMT2(-/-) mice are hypophagic, lean, and have significantly reduced serum leptin levels. This lean phenotype is accompanied by resistance to food-dependent obesity and an increased sensitivity to exogenous leptin administration. PRMT2 colocalizes with STAT3 in hypothalamic nuclei, where it binds and methylates STAT3 through its Ado-Met binding domain. In vitro studies further clarified that the Ado-Met binding domain of PRMT2 induces STAT3 methylation at the Arg31 residue. Absence of PRMT2 results in decreased methylation and prolonged tyrosine phosphorylation of hypothalamic STAT3, which was associated with increased expression of hypothalamic proopiomelanocortin following leptin stimulation.

conclusionsThese data elucidate a molecular pathway that directly links arginine methylation of STAT3 by PRMT2 to the regulation of leptin signaling, suggesting a potential role for PRMT2 antagonism in the treatment of obesity and obesity-related syndromes.

Indexed as

AnimalsArcuate Nucleus of HypothalamusBody WeightEatingEnergy MetabolismGlycogenLeptinLiverMethylationMethyltransferasesMiceMice, Mutant StrainsObesityPhosphorylationProtein-Arginine N-MethyltransferasesProtein Structure, TertiaryGlycogenLeptinMethyltransferasesPRMT2 protein, mouseprotein arginine methyltransferase 2Protein-Arginine N-MethyltransferasesStat3 protein, mouseSTAT3 Transcription Factor

Identifiers

PMID20798359
PMCPMC2997704
OpenAlexW2142075603

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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.