Evidence map›Paper›PMID 30202880›Full record

ArticleNucleic acids research2018

A protein-protein interaction underlies the molecular basis for substrate recognition by an adenosine-to-inosine RNA-editing enzyme.

Suba Rajendren, Aidan C Manning, Haider Al-Awadi, Kentaro Yamada, Yuichiro Takagi, Heather A Hundley

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

29 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The strategies and advances of mRNA translation booster.Asian journal of pharmaceutical sciences · 2025
    Review
  5. ADARs mediate distinct RNA editing activity and gene regulation in thebioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. ADR-2 regulates fertility and oocyte fate inbioRxiv : the preprint server for biology · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Attenuation of Dopaminergic Neurodegeneration in aJournal of developmental biology · 2023
    Article
  16. Review
  17. Article
  18. Review
  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

6 authors at 2 institutions in 1 country.

Suba RajendrenDepartment of Biology, Indiana University, Bloomington, IN 47405, USA.
Aidan C ManningMedical Sciences Program, Indiana University, Bloomington, IN 47405, USA.
Haider Al-AwadiMedical Sciences Program, Indiana University, Bloomington, IN 47405, USA.
Kentaro YamadaDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
Yuichiro TakagiDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
Heather A HundleyMedical Sciences Program, Indiana University, Bloomington, IN 47405, USA.
Indiana University Bloomington · USIndiana University – Purdue University Indianapolis · US

Funding

Mechanism of transcription regulation by the MediatorR01GM111695 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI TAKAGI, YUICHIRO · 2015 to 2019
$1.5M
National Science Foundation MCB-1157688NIGMS NIH HHS R01 GM111695
6 · The paper itself

Abstract

Adenosine deaminases that act on RNA (ADARs) convert adenosine to inosine within double-stranded regions of RNA, resulting in increased transcriptomic diversity, as well as protection of cellular double-stranded RNA (dsRNA) from silencing and improper immune activation. The presence of dsRNA-binding domains (dsRBDs) in all ADARs suggests these domains are important for substrate recognition; however, the role of dsRBDs in vivo remains largely unknown. Herein, our studies indicate the Caenorhabditis elegans ADAR enzyme, ADR-2, has low affinity for dsRNA, but interacts with ADR-1, an editing-deficient member of the ADAR family, which has a 100-fold higher affinity for dsRNA. ADR-1 uses one dsRBD to physically interact with ADR-2 and a second dsRBD to bind to dsRNAs, thereby tethering ADR-2 to substrates. ADR-2 interacts with >1200 transcripts in vivo, and ADR-1 is required for 80% of these interactions. Our results identify a novel mode of substrate recognition for ADAR enzymes and indicate that protein-protein interactions can guide substrate recognition for RNA editors.

Indexed as

RNA EditingAdenosineAdenosine DeaminaseAnimalsAnimals, Genetically ModifiedBinding, CompetitiveCaenorhabditis elegansCaenorhabditis elegans ProteinsDeaminationGene Expression ProfilingInosineMutationProtein BindingRNA, Double-StrandedSubstrate SpecificityAdenosineAdenosine DeaminaseAdr-1 protein, C elegansAdr-2 protein, C elegansCaenorhabditis elegans ProteinsInosineRNA, Double-Stranded

Identifiers

PMID30202880
PMCPMC6182170
OpenAlexW2889715196

What OpenQuestion holds

Textmetadata
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.