Evidence map›Paper›PMID 19289494›Full record

ArticleMolecular and cellular biology2009

A mouse PRMT1 null allele defines an essential role for arginine methylation in genome maintenance and cell proliferation.

Zhenbao Yu, Taiping Chen, Josée Hébert, En Li, Stéphane Richard

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 127 papers.

0numbers the graph read from it
0cells of the map it votes in
127citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

127 citing papers in PubMed, 204 citations in OpenAlex.

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  17. Role of Sam68 in different types of cancer (Review).International journal of molecular medicine · 2025
    Review
  18. Article
  19. Article
  20. Role of PRMT1 and PRMT5 in Breast Cancer.International journal of molecular sciences · 2024
    Review

67 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 5 institutions in 1 country.

Zhenbao YuBloomfield Center for Research on Aging, Segal Cancer Centre, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital, Montréal, Québec, Canada.
Taiping Chen
Josée Hébert
En Li
Stéphane Richard
Hôpital Maisonneuve-Rosemont · CAJewish General Hospital · CALeukemia & Lymphoma Society of Canada · CAMcGill University · CAUniversité de Montréal · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein arginine methyltransferase 1 (PRMT1) is the major enzyme that generates monomethylarginine and asymmetrical dimethylarginine. We report here a conditional null allele of PRMT1 in mice and that the loss of PRMT1 expression leads to embryonic lethality. Using the Cre/lox-conditional system, we show that the loss of PRMT1 in mouse embryonic fibroblasts (MEFs) leads to the loss of arginine methylation of substrates harboring a glycine-arginine rich motif, including Sam68 and MRE11. The loss of PRMT1 in MEFs leads to spontaneous DNA damage, cell cycle progression delay, checkpoint defects, aneuploidy, and polyploidy. We show using a 4-hydroxytamoxifen-inducible Cre that the loss of PRMT1 in MEFs leads to a higher incidence of chromosome losses, gains, structural rearrangements, and polyploidy, as documented by spectral karyotyping. Using PRMT1 small interfering RNA in U2OS cells, we further show that PRMT1-deficient cells are hypersensitive to the DNA damaging agent etoposide and exhibit a defect in the recruitment of the homologous recombination RAD51 recombinase to DNA damage foci. Taken together, these data show that PRMT1 is required for genome integrity and cell proliferation. Our findings also suggest that arginine methylation by PRMT1 is a key posttranslational modification in the DNA damage response pathway in proliferating mammalian cells.

Indexed as

AllelesAdaptor Proteins, Signal TransducingAnimalsArginineCell ProliferationDNADNA-Binding ProteinsDNA DamageDNA Repair EnzymesDown-RegulationEmbryo, MammalianEtoposideFemaleFibroblastsGenomeGenomic InstabilityAdaptor Proteins, Signal TransducingArginineDNADNA-Binding ProteinsDNA Repair EnzymesEtoposideKhdrbs1 protein, mouseMre11a protein, mouseMRE11 Homologue ProteinProtein-Arginine N-MethyltransferasesRad51 protein, mouseRad51 RecombinaseRNA-Binding Proteins

Identifiers

PMID19289494
PMCPMC2681996
OpenAlexW2155408998

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.