Evidence map›Paper›PMID 31685892›Full record

ArticleScientific reports2019

The Protein Arginine Methyltransferases 1 and 5 affect Myc properties in glioblastoma stem cells.

Annarita Favia, Luisa Salvatori, Simona Nanni, Lisa K Iwamoto-Stohl, Sergio Valente, Antonello Mai, Fiorella Scagnoli, Rosaria Anna Fontanella, Pierangela Totta, Sergio Nasi and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

32 citing papers in PubMed, 41 citations in OpenAlex.

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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 2 countries.

Annarita FaviaInstitute of Molecular Biology and Pathology - National Research Council (IBPM-CNR), Rome, Italy.
Luisa SalvatoriInstitute of Molecular Biology and Pathology - National Research Council (IBPM-CNR), Rome, Italy. luisa.salvatori@cnr.it.
Simona NanniInstitute of Medical Pathology, Università Cattolica del Sacro Cuore, Rome, Italy.
Lisa K Iwamoto-StohlUniversity of Cambridge, Cambridge, UK.
Sergio ValenteDepartment of Chemistry and Technologies of Drugs, Sapienza University of Rome, Rome, Italy.
Antonello MaiDepartment of Chemistry and Technologies of Drugs, Sapienza University of Rome, Rome, Italy.ORCID http://orcid.org/0000-0001-9176-2382
Fiorella ScagnoliInstitute of Molecular Biology and Pathology - National Research Council (IBPM-CNR), Rome, Italy.
Rosaria Anna FontanellaInstitute of Molecular Biology and Pathology - National Research Council (IBPM-CNR), Rome, Italy.
Pierangela TottaFutura Stem Cells s.r.l., Rome, Italy.
Sergio NasiInstitute of Molecular Biology and Pathology - National Research Council (IBPM-CNR), Rome, Italy.
Barbara IlliInstitute of Molecular Biology and Pathology - National Research Council (IBPM-CNR), Rome, Italy. barbara.illi@cnr.it.
Institute of Molecular Biology and Pathology · ITIstituto Pasteur · ITSapienza University of Rome · ITUniversità Cattolica del Sacro Cuore · ITUniversity of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein Arginine (R) methylation is the most common post-translational methylation in mammalian cells. Protein Arginine Methyltransferases (PRMT) 1 and 5 dimethylate their substrates on R residues, asymmetrically and symmetrically, respectively. They are ubiquitously expressed and play fundamental roles in tumour malignancies, including glioblastoma multiforme (GBM) which presents largely deregulated Myc activity. Previously, we demonstrated that PRMT5 associates with Myc in GBM cells, modulating, at least in part, its transcriptional properties. Here we show that Myc/PRMT5 protein complex includes PRMT1, in both HEK293T and glioblastoma stem cells (GSCs). We demonstrate that Myc is both asymmetrically and symmetrically dimethylated by PRMT1 and PRMT5, respectively, and that these modifications differentially regulate its stability. Moreover, we show that the ratio between symmetrically and asymmetrically dimethylated Myc changes in GSCs grown in stem versus differentiating conditions. Finally, both PRMT1 and PRMT5 activity modulate Myc binding at its specific target promoters. To our knowledge, this is the first work reporting R asymmetrical and symmetrical dimethylation as novel Myc post-translational modifications, with different functional properties. This opens a completely unexplored field of investigation in Myc biology and suggests symmetrically dimethylated Myc species as novel diagnostic and prognostic markers and druggable therapeutic targets for GBM.

Indexed as

AntibodiesCell Cycle CheckpointsCell DifferentiationCell Line, TumorGlioblastomaHEK293 CellsHumansMethylationNeoplastic Stem CellsPromoter Regions, GeneticProtein-Arginine N-MethyltransferasesProtein BindingProtein StabilityProto-Oncogene Proteins c-mycRepressor ProteinsRNA InterferenceAntibodiesPRMT1 protein, humanPRMT5 protein, humanProtein-Arginine N-MethyltransferasesProto-Oncogene Proteins c-mycRepressor ProteinsRNA, Small InterferingSOX2 protein, humanSOXB1 Transcription Factors

Identifiers

PMID31685892
PMCPMC6828805
OpenAlexW2988905850

What OpenQuestion holds

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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.