Evidence map›Paper›PMID 25662273›Full record

ReviewCellular and molecular life sciences : CMLS2015

The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond.

Nicole Stopa, Jocelyn E Krebs, David Shechter

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 303 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
303citing papers in PubMed, 1 pooled it
14.2field-weighted citation impact, top 1% 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

303 citing papers in PubMed, 1 synthesis or guideline pooled it, 500 citations in OpenAlex.

  1. Pooled it
  2. Article
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  5. RAS-targeted therapies for pancreatic cancer.ESMO gastrointestinal oncology · 2026
    Review
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  9. Review
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  11. Review
  12. Review
  13. Review
  14. Article
  15. PRMT5 is a prognostic-related biomarker associated with the tumor immune microenvironment in lung adenocarcinoma.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026
    Article
  16. Article
  17. Review
  18. Article
  19. Article
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243 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Nicole StopaDepartment of Biological Sciences, University of Alaska Anchorage, 3211 Providence Drive, Anchorage, AK, 99508, USA.
Jocelyn E Krebs
David Shechter
University of Alaska Anchorage · USAlbert Einstein College of Medicine · US

Funding

WORD PROCESSORP30CA013330 · NCI · YESHIVA UNIVERSITY · PI STEVEN C. ALMO · 1985 to 2026
$111.2M
The Administrative CoreP20GM103395 · NIGMS · UNIVERSITY OF ALASKA FAIRBANKS · PI BRIAN M BARNES · 2012 to 2026
$66.1M
PRMT5-MEP50 Histone Arginine Methylation in Early DevelopmentR01GM108646 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI SHECHTER, DAVID · 2014 to 2022
$3.2M
NCI NIH HHS P30 CA013330NIGMS NIH HHS P20 GM103395NIGMS NIH HHS P20GM103395NIGMS NIH HHS R01 GM108646NIGMS NIH HHS R01GM108646
6 · The paper itself

Abstract

Post-translational arginine methylation is responsible for regulation of many biological processes. The protein arginine methyltransferase 5 (PRMT5, also known as Hsl7, Jbp1, Skb1, Capsuleen, or Dart5) is the major enzyme responsible for mono- and symmetric dimethylation of arginine. An expanding literature demonstrates its critical biological function in a wide range of cellular processes. Histone and other protein methylation by PRMT5 regulate genome organization, transcription, stem cells, primordial germ cells, differentiation, the cell cycle, and spliceosome assembly. Metazoan PRMT5 is found in complex with the WD-repeat protein MEP50 (also known as Wdr77, androgen receptor coactivator p44, or Valois). PRMT5 also directly associates with a range of other protein factors, including pICln, Menin, CoPR5 and RioK1 that may alter its subcellular localization and protein substrate selection. Protein substrate and PRMT5-MEP50 post-translation modifications induce crosstalk to regulate PRMT5 activity. Crystal structures of C. elegans PRMT5 and human and frog PRMT5-MEP50 complexes provide substantial insight into the mechanisms of substrate recognition and procession to dimethylation. Enzymological studies of PRMT5 have uncovered compelling insights essential for future development of specific PRMT5 inhibitors. In addition, newly accumulating evidence implicates PRMT5 and MEP50 expression levels and their methyltransferase activity in cancer tumorigenesis, and, significantly, as markers of poor clinical outcome, marking them as potential oncogenes. Here, we review the substantial new literature on PRMT5 and its partners to highlight the significance of understanding this essential enzyme in health and disease.

Indexed as

Adaptor Proteins, Signal TransducingArginineCatalytic DomainCell DifferentiationGene Expression RegulationHistonesHumansMethylationMultiprotein ComplexesNeoplasmsProtein-Arginine N-MethyltransferasesProtein BindingProtein Processing, Post-TranslationalProtein Structure, QuaternaryTranscription FactorsAdaptor Proteins, Signal TransducingArginineHistonesMultiprotein ComplexesPRMT5 protein, humanProtein-Arginine N-MethyltransferasesTranscription FactorsWDR77 protein, human

Identifiers

PMID25662273
PMCPMC4430368
OpenAlexW2066050590

What OpenQuestion holds

Textmetadata
LicenceTDM
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.