Evidence map›Paper›PMID 21447556›Full record

ArticleDevelopment (Cambridge, England)2011

PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in the nuage to silence transposition.

Li Liu, Hongying Qi, Jianquan Wang, Haifan Lin

Open access · bronzeAbstract read
In one paragraph

Article in Development (Cambridge, England), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
13.5field-weighted citation impact, top 1% 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

58 citing papers in PubMed, 114 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Greatwall-Endos-PP2A/B55Open biology · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Germ Granules in Animal Oogenesis.Journal of developmental biology · 2022
    Review
  10. Article
  11. The birth of piRNAs: how mammalian piRNAs are produced, originated, and evolved.Mammalian genome : official journal of the International Mammalian Genome Society · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. 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

4 authors at 1 institution in 1 country.

Li LiuYale Stem Cell Center and Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06509, USA.
Hongying Qi
Jianquan Wang
Haifan Lin
Yale University · US

Funding

REGULATION OF GERMLINE STEM CELL DIVISION IN DROSOPHILAR01HD033760 · NICHD · YALE UNIVERSITY · PI LIN, HAIFAN · 1996 to 2010
$3.6M
Toward a Central Question in Epigenetics: A Major Epigenetic Programming MechanisDP1CA174418 · NCI · YALE UNIVERSITY · PI LIN, HAIFAN · 2012 to 2014
$2.4M
Toward a Central Question in Epigenetics: A Major Epigenetic Programming MechanisDP1OD006825 · OD · YALE UNIVERSITY · PI LIN, HAIFAN · 2010 to 2011
$1.6M
NCI NIH HHS DP1 CA174418NICHD NIH HHS R01 HD033760NICHD NIH HHS R01 HD33760NIH HHS DP1 OD006825NIH HHS DP1-OD006825
6 · The paper itself

Abstract

The nuage is a germline-specific perinuclear structure that remains functionally elusive. Recently, the nuage in Drosophila was shown to contain two of the three PIWI proteins - Aubergine and Argonaute 3 (AGO3) - that are essential for germline development. The PIWI proteins bind to PIWI-interacting RNAs (piRNAs) and function in epigenetic regulation and transposon control. Here, we report a novel nuage component, PAPI (Partner of PIWIs), that contains a TUDOR domain and interacts with all three PIWI proteins via symmetrically dimethylated arginine residues in their N-terminal domain. In adult ovaries, PAPI is mainly cytoplasmic and enriched in the nuage, where it partially colocalizes with AGO3. The localization of PAPI to the nuage does not require the arginine methyltransferase dPRMT5 or AGO3. However, AGO3 is largely delocalized from the nuage and becomes destabilized in the absence of PAPI or dPRMT5, indicating that PAPI recruits PIWI proteins to the nuage to assemble piRNA pathway components. As expected, papi deficiency leads to transposon activation, phenocopying piRNA mutants. This further suggests that PAPI is involved in the piRNA pathway for transposon silencing. Moreover, AGO3 and PAPI associate with the P body component TRAL/ME31B complex in the nuage and transposon activation is observed in tral mutant ovaries. This suggests a physical and functional interaction in the nuage between the piRNA pathway components and the mRNA-degrading P-body components in transposon silencing. Overall, our study reveals a function of the nuage in safeguarding the germline genome against deleterious retrotransposition via the piRNA pathway.

Indexed as

Gene SilencingAnimalsAnimals, Genetically ModifiedArgonaute ProteinsCarrier ProteinsDEAD-box RNA HelicasesDNA Transposable ElementsDrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianFemaleGene Expression Regulation, DevelopmentalGerm CellsMaleModels, BiologicalMutagenesis, InsertionalAGO3 protein, DrosophilaArgonaute ProteinsCarrier ProteinsDEAD-box RNA HelicasesDNA Transposable ElementsDrosophila ProteinsMe31B protein, DrosophilaPAPI protein, drosophilaPeptide Initiation Factorspiwi protein, DrosophilaRibonucleoproteinsRNA-Binding ProteinsRNA-Induced Silencing ComplexTRAL protein, Drosophila

Identifiers

PMID21447556
PMCPMC3074456
OpenAlexW2055654853

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.