Evidence map›Paper›PMID 23778934›Full record

ArticleNucleus (Austin, Tex.)

RpL22e, but not RpL22e-like-PA, is SUMOylated and localizes to the nucleoplasm of Drosophila meiotic spermatocytes.

Michael G Kearse, Jill A Ireland, Smrithi M Prem, Alex S Chen, Vassie C Ware

Open access · goldAbstract read
In one paragraph

Article in Nucleus (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.3field-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

17 citing papers in PubMed, 21 citations in OpenAlex.

  1. 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
  2. Ribosomal protein paralogues in ribosome specialization.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  3. Article
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  5. Article
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  7. Review
  8. Regulation of ribosomal protein genes: An ordered anarchy.Wiley interdisciplinary reviews. RNA · 2021
    Review
  9. Review
  10. Article
  11. 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
  12. Article
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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

5 authors at 2 institutions in 1 country.

Michael G KearseDepartment of Biological Sciences, Lehigh University, Bethlehem, PA, USA.
Jill A Ireland
Smrithi M Prem
Alex S Chen
Vassie C Ware
Bethlehem Area School District · USLehigh University · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Duplicated ribosomal protein (Rp) gene families often encode highly similar or identical proteins with redundant or unique roles. Eukaryotic-specific paralogues RpL22e and RpL22e-like-PA are structurally divergent within the N terminus and differentially expressed, suggesting tissue-specific functions. We previously identified RpL22e-like-PA as a testis Rp. Strikingly, RpL22e is detected in immunoblots at its expected molecular mass (m) of 33 kD and at increasing m of ~43-55 kD, suggesting RpL22e post-translational modification (PTM). Numerous PTMs, including N-terminal SUMOylation, are predicted computationally. Based on S2 cell co-immunoprecipitations, bacterial-based SUMOylation assays and in vivo germline-specific RNAi depletion of SUMO, we conclude that RpL22e is a SUMO substrate. Testis-specific PTMs are evident, including a phosphorylated version of SUMOylated RpL22e identified by in vitro phosphatase experiments. In ribosomal profiles from S2 cells, only unconjugated RpL22e co-sediments with active ribosomes, supporting an extra-translational role for SUMOylated RpL22e. Ectopic expression of an RpL22e N-terminal deletion (lacking SUMO motifs) shows that truncated RpL22e co-sediments with polysomes, implying that RpL22e SUMOylation is dispensable for ribosome biogenesis and function. In mitotic germ cells, both paralogues localize within the cytoplasm and nucleolus. However, within meiotic cells, phase contrast microscopy and co-immunohistochemical analysis with nucleolar markers nucleostemin1 and fibrillarin reveals diffuse nucleoplasmic, but not nucleolar RpL22e localization that transitions to a punctate pattern as meiotic cells mature, suggesting an RpL22e role outside of translation. Germline-specific knockdown of SUMO shows that RpL22e nucleoplasmic distribution is sensitive to SUMO levels, as immunostaining becomes more dispersed. Overall, these data suggest distinct male germline roles for RpL22e and RpL22e-like-PA.

Indexed as

MeiosisProtein Processing, Post-TranslationalAnimalsBiological TransportDrosophila melanogasterDrosophila ProteinsGene Expression Regulation, DevelopmentalIntranuclear SpaceMalePhosphorylationProtein IsoformsRibosomal ProteinsRibosomesRNA-Binding ProteinsSignal TransductionSpermatocytesDrosophila ProteinsProtein IsoformsRibosomal ProteinsRNA-Binding ProteinsRpl22-like protein, DrosophilaRpL22 protein, DrosophilaDrosophiladuplicated ribosomal proteinsmale germlinephosphorylationpost-translational modificationribosomal protein paraloguesRpL22eRpL22e-like-PASUMOylation

Identifiers

PMID23778934
PMCPMC3720754
OpenAlexW2080142330

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.