Evidence map›Paper›PMID 20159986›Full record

ArticleThe Journal of biological chemistry2010

Methylation of ribosomal protein S10 by protein-arginine methyltransferase 5 regulates ribosome biogenesis.

Jinqi Ren, Yaqing Wang, Yuheng Liang, Yongqing Zhang, Shilai Bao, Zhiheng Xu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
4.3field-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

81 citing papers in PubMed, 139 citations in OpenAlex.

  1. Review
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  6. Built differently or defective: can RNA exosomopathies cause ribosome heterogeneity?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  7. Ribosome-associated proteins: unwRAPping ribosome heterogeneity in the twenty-first century.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  8. Article
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21 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

6 authors at 1 institution in 1 country.

Jinqi RenInstitute of Genetics and Developmental Biology, The Key Laboratory of Molecular and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China.
Yaqing Wang
Yuheng Liang
Yongqing Zhang
Shilai Bao
Zhiheng Xu
Chinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Modulation of ribosomal assembly is a fine tuning mechanism for cell number and organ size control. Many ribosomal proteins undergo post-translational modification, but their exact roles remain elusive. Here, we report that ribosomal protein s10 (RPS10) is a novel substrate of an oncoprotein, protein-arginine methyltransferase 5 (PRMT5). We show that PRMT5 interacts with RPS10 and catalyzes its methylation at the Arg(158) and Arg(160) residues. The methylation of RPS10 at Arg(158) and Arg(160) plays a role in the proper assembly of ribosomes, protein synthesis, and optimal cell proliferation. The RPS10-R158K/R160K mutant is not efficiently assembled into ribosomes and is unstable and prone to degradation by the proteasomal pathway. In nucleoli, RPS10 interacts with nucleophosmin/B23 and is predominantly concentrated in the granular component region, which is required for ribosome assembly. The RPS10 methylation mutant interacts weakly with nucleophosmin/B23 and fails to concentrate in the granular component region. Our results suggest that PRMT5 is likely to regulate cell proliferation through the methylation of ribosome proteins, and thus reveal a novel mechanism for PRMT5 in tumorigenesis.

Indexed as

Amino Acid SubstitutionCatalysisCell LineCell ProliferationHumansMethylationMutation, MissenseNuclear ProteinsNucleophosminProtein-Arginine N-MethyltransferasesProtein BiosynthesisProtein MethyltransferasesRibosomal ProteinsRibosomesNPM1 protein, humanNuclear ProteinsNucleophosminPRMT5 protein, humanProtein-Arginine N-MethyltransferasesProtein MethyltransferasesRibosomal Proteinsribosomal protein S10RPS10 protein, human

Identifiers

PMID20159986
PMCPMC2857073
OpenAlexW2005490820

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.