Evidence map›Paper›PMID 21138957›Full record

ArticleNucleic acids research2011

Expression of ribosomal protein L22e family members in Drosophila melanogaster: rpL22-like is differentially expressed and alternatively spliced.

Michael G Kearse, Alex S Chen, Vassie C Ware

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

30 citing papers in PubMed, 46 citations in OpenAlex.

  1. RiboScreenBiomedicines · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Building a case for 'functional identity fraud' in eRpL22 paralogue-specific ribosomes inPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  6. Ribosomal protein paralogues in ribosome specialization.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  7. Article
  8. Article
  9. Ribosome Structural Changes Dynamically Affect Ribosome Function.International journal of molecular sciences · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Ribosome heterogeneity and specialization in development.Wiley interdisciplinary reviews. RNA · 2021
    Review
  14. eLife · 2021
    Article
  15. Review
  16. mSystems · 2020
    Article
  17. Tissue-specific expression of ribosomal protein paralogue eRpL22-like in Drosophila melanogaster eye development.Developmental dynamics : an official publication of the American Association of Anatomists · 2020
    Article
  18. Article
  19. Article
  20. Review
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 1 institution in 1 country.

Michael G KearseDepartment of Biological Sciences, Lehigh University, Bethlehem, PA 18015, USA.
Alex S Chen
Vassie C Ware
Lehigh University · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Several ribosomal protein families contain paralogues whose roles may be equivalent or specialized to include extra-ribosomal functions. RpL22e family members rpL22 and rpL22-like are differentially expressed in Drosophila melanogaster: rpL22-like mRNA is gonad specific whereas rpL22 is expressed ubiquitously, suggesting distinctive paralogue functions. To determine if RpL22-like has a divergent role in gonads, rpL22-like expression was analysed by qRT-PCR and western blots, respectively, showing enrichment of rpL22-like mRNA and a 34 kDa (predicted) protein in testis, but not in ovary. Immunohistochemistry of the reproductive tract corroborated testis-specific expression. RpL22-like detection in 80S/polysome fractions from males establishes a role for this tissue-specific paralogue as a ribosomal component. Unpredictably, expression profiles revealed a low abundant, alternative mRNA variant (designated 'rpL22-like short') that would encode a novel protein lacking the C-terminal ribosomal protein signature but retaining part of the N-terminal domain. This variant results from splicing of a retained intron (defined by non-canonical splice sites) within rpL22-like mRNA. Polysome association and detection of a low abundant 13.5 kDa (predicted) protein in testis extracts suggests variant mRNA translation. Collectively, our data show that alternative splicing of rpL22-like generates structurally distinct protein products: ribosomal component RpL22-like and a novel protein with a role distinct from RpL22-like.

Indexed as

Alternative SplicingAmino Acid SequenceAnimalsBase SequenceDrosophila melanogasterDrosophila ProteinsMaleMolecular Sequence DataPolyribosomesProtein BiosynthesisRibosomal ProteinsRibosomesRNA-Binding ProteinsRNA, MessengerSequence Homology, Amino AcidTestisDrosophila ProteinsRibosomal ProteinsRNA-Binding ProteinsRNA, MessengerRpl22-like protein, DrosophilaRpL22 protein, Drosophila

Identifiers

PMID21138957
PMCPMC3074143
OpenAlexW1988082673

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.