Evidence map›Paper›PMID 28074910›Full record

ArticleScientific reports2017

Myosin phosphatase and RhoA-activated kinase modulate arginine methylation by the regulation of protein arginine methyltransferase 5 in hepatocellular carcinoma cells.

Adrienn Sipos, Judit Iván, Bálint Bécsi, Zsuzsanna Darula, István Tamás, Dániel Horváth, Katalin F Medzihradszky, Ferenc Erdődi, Beáta Lontay

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Dysregulation of arginine methylation in tumorigenesis.Frontiers in molecular biosciences · 2024
    Review
  5. Protein arginine methylation in viral infection and antiviral immunity.International journal of biological sciences · 2023
    Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Role of PRMT5 in bladder cancer: a comprehensive study.Translational cancer research · 2019
    Article
  15. Induction of DUSP14 ubiquitination by PRMT5-mediated arginine methylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  16. Article
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

9 authors.

Adrienn SiposDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Debrecen, H-4032, Hungary.
Judit IvánDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Debrecen, H-4032, Hungary.
Bálint BécsiDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Debrecen, H-4032, Hungary.
Zsuzsanna DarulaLaboratory of Proteomics Research, Biological Research Centre, Hungarian Academy of Sciences, Szeged, H-6726, Hungary.
István TamásDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Debrecen, H-4032, Hungary.
Dániel HorváthDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Debrecen, H-4032, Hungary.
Katalin F MedzihradszkyLaboratory of Proteomics Research, Biological Research Centre, Hungarian Academy of Sciences, Szeged, H-6726, Hungary.
Ferenc ErdődiDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Debrecen, H-4032, Hungary.
Beáta LontayDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Debrecen, H-4032, Hungary.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myosin phosphatase (MP) holoenzyme is a protein phosphatase-1 (PP1) type Ser/Thr specific enzyme that consists of a PP1 catalytic (PP1c) and a myosin phosphatase target subunit-1 (MYPT1). MYPT1 is an ubiquitously expressed isoform and it targets PP1c to its substrates. We identified the protein arginine methyltransferase 5 (PRMT5) enzyme of the methylosome complex as a MYPT1-binding protein uncovering the nuclear MYPT1-interactome of hepatocellular carcinoma cells. It is shown that PRMT5 is regulated by phosphorylation at Thr80 by RhoA-associated protein kinase and MP. Silencing of MYPT1 increased the level of the PRMT5-specific symmetric dimethylation on arginine residues of histone 2 A/4, a repressing gene expression mark, and it resulted in a global change in the expression of genes affecting cellular processes like growth, proliferation and cell death, also affecting the expression of the retinoblastoma protein and c-Myc. The phosphorylation of the MP inhibitory MYPT1

Indexed as

ArginineCarcinoma, HepatocellularCell Line, TumorCell NucleusDown-RegulationGene Expression Regulation, NeoplasticGene SilencingHep G2 CellsHumansLiver NeoplasmsMethylationModels, BiologicalMyosin-Light-Chain PhosphataseOligonucleotide Array Sequence AnalysisPhosphorylationPhosphothreonineArginineMyosin-Light-Chain PhosphatasePhosphothreoninePRMT5 protein, humanProtein-Arginine N-Methyltransferasesrho-Associated Kinases

Identifiers

PMID28074910
PMCPMC5225440

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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.