Evidence map›Paper›PMID 30692633›Full record

ArticleOncogene2019

The arginine methyltransferase PRMT1 regulates IGF-1 signaling in breast cancer.

Ali Choucair, Thuy Ha Pham, Soleilmane Omarjee, Julien Jacquemetton, Loay Kassem, Olivier Trédan, Juliette Rambaud, Elisabetta Marangoni, Laura Corbo, Isabelle Treilleux and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Oncogene, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.0field-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

33 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
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  7. Role of PRMT1 and PRMT5 in Breast Cancer.International journal of molecular sciences · 2024
    Review
  8. Article
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  14. A Basic Review on Estrogen Receptor Signaling Pathways in Breast Cancer.International journal of molecular sciences · 2023
    Review
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  17. Article
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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 5 institutions in 3 countries.

Ali ChoucairINSERM U1052, Centre de Recherche en Cancérologie de Lyon, Lyon, France.
Thuy Ha PhamINSERM U1052, Centre de Recherche en Cancérologie de Lyon, Lyon, France.
Soleilmane OmarjeeINSERM U1052, Centre de Recherche en Cancérologie de Lyon, Lyon, France.
Julien JacquemettonINSERM U1052, Centre de Recherche en Cancérologie de Lyon, Lyon, France.
Loay KassemClinical Oncology Department, Faculty of Medicine, Cairo University, Cairo, Egypt.
Olivier TrédanOncology Department, Centre Leon Bérard, Lyon, France.
Juliette RambaudINSERM U1052, Centre de Recherche en Cancérologie de Lyon, Lyon, France.
Elisabetta MarangoniTranslational Research Department, Institut Curie, 75005, Paris, France.
Laura CorboINSERM U1052, Centre de Recherche en Cancérologie de Lyon, Lyon, France.
Isabelle TreilleuxINSERM U1052, Centre de Recherche en Cancérologie de Lyon, Lyon, France.
Muriel Le RomancerINSERM U1052, Centre de Recherche en Cancérologie de Lyon, Lyon, France. muriel.leromancer@lyon.unicancer.fr.
Université Claude Bernard Lyon 1 · FRCentre National de la Recherche Scientifique · FRCentre Léon Bérard · FRCairo University · EGInstitut Curie · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aside from its well-known nuclear routes of signaling, estrogen also mediates its effects through cytoplasmic signaling. Estrogen signaling involves numerous posttranslational modifications of its receptor ERα, the best known being phosphorylation. Our research group previously showed that upon estrogen stimulation, ERα is methylated on residue R260 and forms the mERα/Src/PI3K complex, central to the rapid transduction of nongenomic estrogen signals. Regulation of ERα signaling via its phosphorylation by growth factors is well recognized, and we wondered whether they could also trigger ERα methylation (mERα). Here, we found that IGF-1 treatment of MCF-7 cells induced rapid ERα methylation by the arginine methyltransferase PRMT1 and triggered the binding of mERα to IGF-1R. Mechanistically, we showed that PRMT1 bound constitutively to IGF-1R and that PRMT1 became activated upon IGF-1 stimulation. Moreover, we found that expression or pharmacological inhibition of PRMT1 impaired mERα and IGF-1 signaling. Our findings were substantiated in a cohort of breast tumors in which IGF-1R expression was positively correlated with ERα/Src and ERα/PI3K expression, hallmarks of nongenomic estrogen signaling, reinforcing the link between IGF-1R and mERα. Altogether, these results provide a new insight into ERα and IGF-1R interference, and open novel perspectives for combining endocrine therapies with PRMT1 inhibitors in ERα-positive tumors.

Indexed as

Breast NeoplasmsCell Line, TumorEstrogen Receptor alphaEstrogensFemaleGenes, srcHumansInsulin-Like Growth Factor IMCF-7 CellsMethylationPhosphatidylinositol 3-KinasesProtein-Arginine N-MethyltransferasesProtein BindingReceptor, IGF Type 1Repressor ProteinsSignal TransductionEstrogen Receptor alphaEstrogensIGF1 protein, humanInsulin-Like Growth Factor IPhosphatidylinositol 3-KinasesPRMT1 protein, humanProtein-Arginine N-MethyltransferasesReceptor, IGF Type 1Repressor Proteins

Identifiers

PMID30692633
PMCPMC6755991
OpenAlexW2912880260

What OpenQuestion holds

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LicenceCC BY
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.