Evidence map›Paper›PMID 31384064›Full record

ArticleNature structural & molecular biology2019

The nascent RNA binding complex SFiNX licenses piRNA-guided heterochromatin formation.

Julia Batki, Jakob Schnabl, Juncheng Wang, Dominik Handler, Veselin I Andreev, Christian E Stieger, Maria Novatchkova, Lisa Lampersberger, Kotryna Kauneckaite, Wei Xie and 3 more

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed, 1 pooled it
19.2field-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

69 citing papers in PubMed, 1 synthesis or guideline pooled it, 107 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. piRNA direct the chromatin reader to its genomic targets.bioRxiv : the preprint server for biology · 2026
    Article
  8. Rapid evolution and comparative analysis of piRNA clusters inbioRxiv : the preprint server for biology · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. H3K14ac facilitates the reinstallation of constitutive heterochromatin inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Review
  19. Article
  20. Review

9 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

13 authors at 2 institutions in 2 countries.

Julia BatkiInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna BioCenter, Vienna, Austria.
Jakob SchnablInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna BioCenter, Vienna, Austria.
Juncheng WangStructural Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY, USA.ORCID http://orcid.org/0000-0003-1696-1052
Dominik HandlerInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna BioCenter, Vienna, Austria.
Veselin I AndreevInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna BioCenter, Vienna, Austria.
Christian E StiegerInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna BioCenter, Vienna, Austria.
Maria NovatchkovaInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna BioCenter, Vienna, Austria.
Lisa LampersbergerInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna BioCenter, Vienna, Austria.
Kotryna KauneckaiteInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna BioCenter, Vienna, Austria.
Wei XieStructural Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY, USA.ORCID http://orcid.org/0000-0002-4550-6211
Karl MechtlerInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna BioCenter, Vienna, Austria.
Dinshaw J PatelStructural Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY, USA.ORCID http://orcid.org/0000-0002-9779-7778
Julius BrenneckeInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna BioCenter, Vienna, Austria. julius.brennecke@imba.oeaw.ac.at.ORCID http://orcid.org/0000-0002-5141-0814
Institute of Molecular Biotechnology · ATMemorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI MALCOLM S. CAPEL · 2018 to 2026
$34.2M
ExRNA composition in SLE patients and factors influencing exRNP abundance and thU19CA179564 · NCI · ROCKEFELLER UNIVERSITY · PI TUSCHL, THOMAS · 2013 to 2017
$7.1M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
NCI NIH HHS P30 CA008748NCI NIH HHS U19 CA179564NCRR NIH HHS S10 RR029205NIGMS NIH HHS P30 GM124165
6 · The paper itself

Abstract

The PIWI-interacting RNA (piRNA) pathway protects genome integrity in part through establishing repressive heterochromatin at transposon loci. Silencing requires piRNA-guided targeting of nuclear PIWI proteins to nascent transposon transcripts, yet the subsequent molecular events are not understood. Here, we identify SFiNX (silencing factor interacting nuclear export variant), an interdependent protein complex required for Piwi-mediated cotranscriptional silencing in Drosophila. SFiNX consists of Nxf2-Nxt1, a gonad-specific variant of the heterodimeric messenger RNA export receptor Nxf1-Nxt1 and the Piwi-associated protein Panoramix. SFiNX mutant flies are sterile and exhibit transposon derepression because piRNA-loaded Piwi is unable to establish heterochromatin. Within SFiNX, Panoramix recruits heterochromatin effectors, while the RNA binding protein Nxf2 licenses cotranscriptional silencing. Our data reveal how Nxf2 might have evolved from an RNA transport receptor into a cotranscriptional silencing factor. Thus, NXF variants, which are abundant in metazoans, can have diverse molecular functions and might have been coopted for host genome defense more broadly.

Indexed as

Amino Acid SequenceAnimalsArgonaute ProteinsBinding SitesCrystallography, X-RayDNA Transposable ElementsDrosophila melanogasterDrosophila ProteinsGene Expression RegulationGene SilencingGenome, InsectHeterochromatinModels, MolecularMultiprotein ComplexesNuclear ProteinsNucleocytoplasmic Transport ProteinsArgonaute ProteinsDNA Transposable ElementsDrosophila ProteinsHeterochromatinMultiprotein ComplexesNuclear ProteinsNucleocytoplasmic Transport Proteinsnxf2 protein, Drosophilapanx protein, Drosophilapiwi protein, DrosophilaRNA-Binding ProteinsRNA, Small InterferingSBR protein, Drosophila

Identifiers

PMID31384064
PMCPMC6828549
OpenAlexW2955982482

What OpenQuestion holds

Textmetadata
LicenceTDM
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.