Evidence map›Paper›PMID 28683311›Full record

ArticleCell reports2017

Argonaute Utilization for miRNA Silencing Is Determined by Phosphorylation-Dependent Recruitment of LIM-Domain-Containing Proteins.

Katherine S Bridge, Kunal M Shah, Yigen Li, Daniel E Foxler, Sybil C K Wong, Duncan C Miller, Kathryn M Davidson, John G Foster, Ruth Rose, Michael R Hodgkinson and 8 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

43 citing papers in PubMed, 65 citations in OpenAlex.

  1. ClonalLife science alliance · 2026
    Article
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  3. Review
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  7. Article
  8. Review
  9. Article
  10. Article
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  12. AGO2 silences mobile transposons in the nucleus of quiescent cells.Nature structural & molecular biology · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. The Multiplicity of Argonaute Complexes in Mammalian Cells.The Journal of pharmacology and experimental therapeutics · 2023
    Review
  17. Article
  18. Article
  19. Interplay between K-RAS and miRNAs.Trends in cancer · 2022
    Review
  20. Regulation of MicroRNAs.Methods in molecular biology (Clifton, N.J.) · 2022
    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

18 authors at 6 institutions in 3 countries.

Katherine S BridgeCentre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
Kunal M ShahCentre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
Yigen LiCentre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
Daniel E FoxlerCentre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
Sybil C K WongCentre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
Duncan C MillerCentre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
Kathryn M DavidsonCentre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
John G FosterCentre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
Ruth RoseSchool of Biological and Chemical Sciences, Queen Mary University of London, Fogg Building, Mile End Road, London E1 4NS, UK.
Michael R HodgkinsonDepartment of Biology, University of York, Heslington, York YO10 5DD, UK.
Paulo S RibeiroCentre for Tumour Biology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
A Aziz AboobakerDepartment of Zoology, University of Oxford, The Tinbergen Building, South Parks Road, Oxford OX1 3PS, UK.
Kenta YashiroCardiac Regeneration and Therapeutics, Osaka University Graduate School of Medicine, 2-2 Yamada-oka, Suita, Osaka 565-0871, Japan.
Xiaozhong WangDepartment of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208, USA.
Paul R GravesDepartment of Radiation Oncology, New York-Presbyterian Brooklyn Methodist Hospital, 506 6th Street, Brooklyn, NY 11215, USA.
Michael J PlevinDepartment of Biology, University of York, Heslington, York YO10 5DD, UK.
Dimitris LagosCentre for Immunology and Infection, Hull York Medical School and Department of Biology, University of York, Heslington, York YO10 5DD, UK.
Tyson V SharpCentre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK. Electronic address: t.sharp@qmul.ac.uk.
Queen Mary University of London · GBUniversity of York · GBNewYork–Presbyterian Brooklyn Methodist Hospital · USNorthwestern University · USOsaka University · JPUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/I007571/1Cancer Research UK 12733Medical Research Council MR/L008505/1Medical Research Council MR/N009185/1
6 · The paper itself

Abstract

As core components of the microRNA-induced silencing complex (miRISC), Argonaute (AGO) proteins interact with TNRC6 proteins, recruiting other effectors of translational repression/mRNA destabilization. Here, we show that LIMD1 coordinates the assembly of an AGO-TNRC6 containing miRISC complex by binding both proteins simultaneously at distinct interfaces. Phosphorylation of AGO2 at Ser 387 by Akt3 induces LIMD1 binding, which in turn enables AGO2 to interact with TNRC6A and downstream effector DDX6. Conservation of this serine in AGO1 and 4 indicates this mechanism may be a fundamental requirement for AGO function and miRISC assembly. Upon CRISPR-Cas9-mediated knockout of LIMD1, AGO2 miRNA-silencing function is lost and miRNA silencing becomes dependent on a complex formed by AGO3 and the LIMD1 family member WTIP. The switch to AGO3 utilization occurs due to the presence of a glutamic acid residue (E390) on the interaction interface, which allows AGO3 to bind to LIMD1, AJUBA, and WTIP irrespective of Akt signaling.

Indexed as

Gene SilencingArgonaute ProteinsAutoantigensDEAD-box RNA HelicasesHEK293 CellsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsMicroRNAsPhosphorylationProtein BindingProtein Processing, Post-TranslationalProto-Oncogene ProteinsRNA-Binding ProteinsAGO2 protein, humanArgonaute ProteinsAutoantigensDDX6 protein, humanDEAD-box RNA HelicasesIntracellular Signaling Peptides and ProteinsLIMD1 protein, humanLIM Domain ProteinsMicroRNAsProto-Oncogene ProteinsRNA-Binding ProteinsTNRC6A protein, humanAGO2AKTArgonauteDDX6GW182LIMD1microRNAmiRISCTNRC6AWTIP

Identifiers

PMID28683311
PMCPMC5507773
OpenAlexW2732184391

What OpenQuestion holds

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LicenceCC BY
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.