Evidence map›Paper›PMID 25822791›Full record

ArticleNature2015

Defining fundamental steps in the assembly of the Drosophila RNAi enzyme complex.

Shintaro Iwasaki, Hiroshi M Sasaki, Yuriko Sakaguchi, Tsutomu Suzuki, Hisashi Tadakuma, Yukihide Tomari

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

81 citing papers in PubMed, 138 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. The biogenesis and regulation of animal microRNAs.Nature reviews. Molecular cell biology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Size-Selective Capturing of Exosomes Using DNA Tripods.Journal of the American Chemical Society · 2024
    Article
  13. Review
  14. Article
  15. Review
  16. Hsp70 and Hsp90 Elaborately Regulate RNAi Efficiency inInternational journal of molecular sciences · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Article

21 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

6 authors at 1 institution in 1 country.

Shintaro IwasakiInstitute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.
Hiroshi M SasakiInstitute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.
Yuriko SakaguchiDepartment of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Tsutomu SuzukiDepartment of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Hisashi TadakumaDepartment of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.
Yukihide Tomari1] Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan. [2] Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.
The University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small RNAs such as small interfering RNAs (siRNAs) and microRNAs (miRNAs) silence the expression of their complementary target messenger RNAs via the formation of effector RNA-induced silencing complexes (RISCs), which contain Argonaute (Ago) family proteins at their core. Although loading of siRNA duplexes into Drosophila Ago2 requires the Dicer-2-R2D2 heterodimer and the Hsc70/Hsp90 (Hsp90 also known as Hsp83) chaperone machinery, the details of RISC assembly remain unclear. Here we reconstitute RISC assembly using only Ago2, Dicer-2, R2D2, Hsc70, Hsp90, Hop, Droj2 (an Hsp40 homologue) and p23. By following the assembly of single RISC molecules, we find that, in the absence of the chaperone machinery, an siRNA bound to Dicer-2-R2D2 associates with Ago2 only transiently. The chaperone machinery extends the dwell time of the Dicer-2-R2D2-siRNA complex on Ago2, in a manner dependent on recognition of the 5'-phosphate on the siRNA guide strand. We propose that the chaperone machinery supports a productive state of Ago2, allowing it to load siRNA duplexes from Dicer-2-R2D2 and thereby assemble RISC.

Indexed as

RNA InterferenceAnimalsArgonaute ProteinsDrosophila melanogasterDrosophila ProteinsHeat-Shock ProteinsIn Vitro TechniquesJanus KinasesProtein BindingRibonuclease IIIRNA-Binding ProteinsRNA, Guide, CRISPR-Cas SystemsRNA HelicasesRNA-Induced Silencing ComplexRNA, Small InterferingTranscription FactorsAGO2 protein, DrosophilaArgonaute ProteinsDCR-2 protein, DrosophilaDrosophila ProteinsHeat-Shock Proteinshop protein, DrosophilaJanus KinasesR2D2 protein, DrosophilaRibonuclease IIIRNA-Binding ProteinsRNA, Guide, CRISPR-Cas SystemsRNA HelicasesRNA-Induced Silencing ComplexRNA, Small InterferingTranscription Factors

Identifiers

PMID25822791
OpenAlexW2045437345

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.