Evidence map›Paper›PMID 26446993›Full record

ArticleNucleic acids research2015

Control of the localization and function of a miRNA silencing component TNRC6A by Argonaute protein.

Kenji Nishi, Tomoko Takahashi, Masataka Suzawa, Takuya Miyakawa, Tatsuya Nagasawa, Yvelt Ming, Masaru Tanokura, Kumiko Ui-Tei

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. The roles of subcellular Argonaute 2 in cardiovascular diseases.Journal of translational internal medicine · 2025
    Article
  4. Review
  5. Review
  6. Review
  7. Nuclear miRNAs: Gene Regulation Activities.International journal of molecular sciences · 2024
    Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  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

8 authors at 1 institution in 1 country.

Kenji NishiDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan.
Tomoko TakahashiDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan.
Masataka SuzawaDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan.
Takuya MiyakawaDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan.
Tatsuya NagasawaDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan.
Yvelt MingDepartment of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, University of Tokyo, Chiba-ken 277-8651, Japan.
Masaru TanokuraDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan.
Kumiko Ui-TeiDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, University of Tokyo, Chiba-ken 277-8651, Japan ktei@bs.s.u-tokyo.ac.jp.
The University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GW182 family proteins play important roles in microRNA (miRNA)-mediated RNA silencing. They directly interact with Argonaute (Ago) proteins in processing bodies (P bodies), cytoplasmic foci involved in mRNA degradation and storage. Recently, we revealed that a human GW182 family protein, TNRC6A, is a nuclear-cytoplasmic shuttling protein, and its subcellular localization is regulated by its own nuclear localization signal and nuclear export signal. Regarding the further controlling mechanism of TNRC6A subcellular localization, we found that TNRC6A protein is tethered in P bodies by direct interaction with Ago2 under Ago2 overexpression condition in HeLa cells. Furthermore, it was revealed that such Ago proteins might be strongly tethered in the P bodies through Ago-bound small RNAs. Thus, our results indicate that TNRC6A subcellular localization is substantially controlled by the interaction with Ago proteins. Furthermore, it was also revealed that the TNRC6A subcellular localization affects the RNA silencing activity.

Indexed as

RNA InterferenceActive Transport, Cell NucleusAmino Acid MotifsArgonaute ProteinsAutoantigensCell NucleusCytoplasmHeLa CellsHumansMicroRNAsMutationRNA-Binding ProteinsRNA, Small UntranslatedTransfectionAGO2 protein, humanArgonaute ProteinsAutoantigensMicroRNAsRNA-Binding ProteinsRNA, Small UntranslatedTNRC6A protein, human

Identifiers

PMID26446993
PMCPMC4787778
OpenAlexW2175457304

What OpenQuestion holds

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LicenceCC BY-NC
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.