Evidence map›Paper›PMID 23990801›Full record

ArticlePLoS genetics2013

The ribosomal protein Rpl22 controls ribosome composition by directly repressing expression of its own paralog, Rpl22l1.

Monique N O'Leary, Katherine H Schreiber, Yong Zhang, Anne-Cécile E Duc, Shuyun Rao, J Scott Hale, Emmeline C Academia, Shreya R Shah, John F Morton, Carly A Holstein and 7 more

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

87 citing papers in PubMed, 138 citations in OpenAlex.

  1. Article
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  9. Review
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  14. Ribosome specialization by cancer-associated ribosomal protein mutations: progress made and open questions.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  15. Ribosomal protein paralogues in ribosome specialization.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  16. Article
  17. Article
  18. Article
  19. A dual ribosomal system in the zebrafish soma and germline.bioRxiv : the preprint server for biology · 2024
    Article
  20. Article

27 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

17 authors at 4 institutions in 1 country.

Monique N O'LearyDepartment of Biochemistry, University of Washington, Seattle, Washington, United States of America.
Katherine H Schreiber
Yong Zhang
Anne-Cécile E Duc
Shuyun Rao
J Scott Hale
Emmeline C Academia
Shreya R Shah
John F Morton
Carly A Holstein
Dan B Martin
Matt Kaeberlein
Warren C Ladiges
Pamela J Fink
Vivian L Mackay
David L Wiest
Brian K Kennedy
University of Washington · USFox Chase Cancer Center · USBuck Institute for Research on Aging · USInstitute for Systems Biology · US

Funding

CHARACTERIZATION OF RECENT THYMIC EMIGRANTSR01AI064318 · NIAID · UNIVERSITY OF WASHINGTON · PI URDAHL, KEVIN B · 2005 to 2019
$5.8M
TOR, Translation and AgingR01AG033373 · NIA · UNIVERSITY OF WASHINGTON · PI KENNEDY, BRIAN K · 2009 to 2013
$1.8M
Characterization of Recent Thymic EmigrantsR56AI064318 · NIAID · UNIVERSITY OF WASHINGTON · PI FINK, PAMELA J · 2014 to 2014
$429k
NIAID NIH HHS R01 AI064318NIAID NIH HHS R56 AI064318NIA NIH HHS R01 AG033373
6 · The paper itself

Abstract

Most yeast ribosomal protein genes are duplicated and their characterization has led to hypotheses regarding the existence of specialized ribosomes with different subunit composition or specifically-tailored functions. In yeast, ribosomal protein genes are generally duplicated and evidence has emerged that paralogs might have specific roles. Unlike yeast, most mammalian ribosomal proteins are thought to be encoded by a single gene copy, raising the possibility that heterogenous populations of ribosomes are unique to yeast. Here, we examine the roles of the mammalian Rpl22, finding that Rpl22(-/-) mice have only subtle phenotypes with no significant translation defects. We find that in the Rpl22(-/-) mouse there is a compensatory increase in Rpl22-like1 (Rpl22l1) expression and incorporation into ribosomes. Consistent with the hypothesis that either ribosomal protein can support translation, knockdown of Rpl22l1 impairs growth of cells lacking Rpl22. Mechanistically, Rpl22 regulates Rpl22l1 directly by binding to an internal hairpin structure and repressing its expression. We propose that ribosome specificity may exist in mammals, providing evidence that one ribosomal protein can influence composition of the ribosome by regulating its own paralog.

Indexed as

Sequence Homology, Amino AcidAmino Acid SequenceAnimalsGene Expression RegulationMiceMolecular Sequence DataProtein BiosynthesisRibosomal ProteinsRibosomesRNARNA-Binding ProteinsRibosomal ProteinsRNARNA-Binding ProteinsRPL22L1 protein, mouseRPL22 protein, mouse

Identifiers

PMID23990801
PMCPMC3750023
OpenAlexW2044745732

What OpenQuestion holds

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LicenceCC BY
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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.