Evidence map›Paper›PMID 27697862›Full record

ArticleMolecular and cellular biology2016

Human PDCD2L Is an Export Substrate of CRM1 That Associates with 40S Ribosomal Subunit Precursors.

Anne-Marie Landry-Voyer, Sarah Bilodeau, Danny Bergeron, Kiersten L Dionne, Sarah A Port, Caroline Rouleau, François-Michel Boisvert, Ralph H Kehlenbach, François Bachand

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Biallelic variants in the conserved ribosomal protein chaperone geneProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Programmed Cell Death 2-Like (G3 (Bethesda, Md.) · 2020
    Article
  17. Article
  18. Article
  19. Review
  20. 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 at 2 institutions in 2 countries.

Anne-Marie Landry-VoyerRNA Group, Department of Biochemistry, Université de Sherbrooke, Sherbrooke, Québec, Canada.
Sarah BilodeauRNA Group, Department of Biochemistry, Université de Sherbrooke, Sherbrooke, Québec, Canada.
Danny BergeronRNA Group, Department of Biochemistry, Université de Sherbrooke, Sherbrooke, Québec, Canada.
Kiersten L DionneRNA Group, Department of Biochemistry, Université de Sherbrooke, Sherbrooke, Québec, Canada.
Sarah A PortDepartment of Molecular Biology, Faculty of Medicine, GZMB, Georg August University Göttingen, Göttingen, Germany.
Caroline RouleauRNA Group, Department of Biochemistry, Université de Sherbrooke, Sherbrooke, Québec, Canada.
François-Michel BoisvertDepartment of Anatomy and Cell Biology, Université de Sherbrooke, Sherbrooke, Québec, Canada.
Ralph H KehlenbachDepartment of Molecular Biology, Faculty of Medicine, GZMB, Georg August University Göttingen, Göttingen, Germany.
François BachandRNA Group, Department of Biochemistry, Université de Sherbrooke, Sherbrooke, Québec, Canada f.bachand@usherbrooke.ca.
Université de Sherbrooke · CAUniversity of Göttingen · DE

Funding

CIHR MOP-273292
6 · The paper itself

Abstract

Protein arginine methyltransferase 3 (PRMT3) forms a stable complex with 40S ribosomal protein S2 (RPS2) and contributes to ribosome biogenesis. However, the molecular mechanism by which PRMT3 influences ribosome biogenesis and/or function still remains unclear. Using quantitative proteomics, we identified human programmed cell death 2-like (PDCD2L) as a novel PRMT3-associated protein. Our data suggest that RPS2 promotes the formation of a conserved extraribosomal complex with PRMT3 and PDCD2L. We also show that PDCD2L associates with 40S subunit precursors that contain a 3'-extended form of the 18S rRNA (18S-E pre-rRNA) and several pre-40S maturation factors. PDCD2L shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner using a leucine-rich nuclear export signal that is sufficient to direct the export of a reporter protein. Although PDCD2L is not required for the biogenesis and export of 40S ribosomal subunits, we found that PDCD2L-null cells accumulate free 60S ribosomal subunits, which is indicative of a deficiency in 40S subunit availability. Our data also indicate that PDCD2L and its paralog, PDCD2, function redundantly in 40S ribosomal subunit production. Our findings uncover the existence of an extraribosomal complex consisting of PDCD2L, RPS2, and PRMT3 and support a role for PDCD2L in the late maturation of 40S ribosomal subunits.

Indexed as

Apoptosis Regulatory ProteinsCarrier ProteinsCell Line, TumorCell NucleusCytoplasmHEK293 CellsHeLa CellsHumansMass SpectrometryProtein-Arginine N-MethyltransferasesProtein BindingProteomicsRibosomal ProteinsRNA-Binding ProteinsApoptosis Regulatory ProteinsCarrier ProteinsPDCD2L protein, humanPRMT3 protein, humanProtein-Arginine N-MethyltransferasesRibosomal ProteinsRNA-Binding ProteinsRPS2 protein, human

Identifiers

PMID27697862
PMCPMC5126290
OpenAlexW2529422974

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.