Evidence map›Paper›PMID 38613392›Full record

ArticleNucleic acids research2024

Interaction between a J-domain co-chaperone and a specific Argonaute protein contributes to microRNA function in animals.

Pierre-Marc Frédérick, Guillaume Jannot, Isabelle Banville, Martin J Simard

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

3 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. Review
  3. 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

4 authors at 1 institution in 1 country.

Pierre-Marc FrédérickOncology Division, CHU de Québec-Université Laval Research Center, Québec, QC G1R 3S3, Canada.
Guillaume JannotOncology Division, CHU de Québec-Université Laval Research Center, Québec, QC G1R 3S3, Canada.
Isabelle BanvilleOncology Division, CHU de Québec-Université Laval Research Center, Québec, QC G1R 3S3, Canada.
Martin J SimardOncology Division, CHU de Québec-Université Laval Research Center, Québec, QC G1R 3S3, Canada.ORCID 0000-0002-3189-9309
Université Laval · CA

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Aric L Daul, Ann E. Rougvie · 2012 to 2026
$7.5M
CIHR MOP-142241NIH HHS P40 OD010440
6 · The paper itself

Abstract

MicroRNAs (miRNAs) are essential regulators of several biological processes. They are loaded onto Argonaute (AGO) proteins to achieve their repressive function, forming the microRNA-Induced Silencing Complex known as miRISC. While several AGO proteins are expressed in plants and animals, it is still unclear why specific AGOs are strictly binding miRNAs. Here, we identified the co-chaperone DNJ-12 as a new interactor of ALG-1, one of the two major miRNA-specific AGOs in Caenorhabditis elegans. DNJ-12 does not interact with ALG-2, the other major miRNA-specific AGO, and PRG-1 and RDE-1, two AGOs involved in other small RNA pathways, making it a specific actor in ALG-1-dependent miRNA-mediated gene silencing. The loss of DNJ-12 causes developmental defects associated with defective miRNA function. Using the Auxin Inducible Degron system, a powerful tool to acutely degrade proteins in specific tissues, we show that DNJ-12 depletion hampers ALG-1 interaction with HSP70, a chaperone required for miRISC loading in vitro. Moreover, DNJ-12 depletion leads to the decrease of several miRNAs and prevents their loading onto ALG-1. This study uncovers the importance of a co-chaperone for the miRNA function in vivo and provides insights to explain how different small RNAs associate with specific AGO in animals.

Indexed as

Argonaute ProteinsCaenorhabditis elegansCaenorhabditis elegans ProteinsHSP40 Heat-Shock ProteinsMicroRNAsMolecular ChaperonesAnimalsHSP70 Heat-Shock ProteinsProtein BindingRNA-Binding ProteinsALG-1 protein, C elegansArgonaute ProteinsCaenorhabditis elegans ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMicroRNAsMolecular ChaperonesRNA-Binding Proteins

Identifiers

PMID38613392
PMCPMC11194074
OpenAlexW4394785868

What OpenQuestion holds

Textmetadata
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.