Evidence map›Paper›PMID 29554310›Full record

ArticleNucleic acids research2018

4EHP-independent repression of endogenous mRNAs by the RNA-binding protein GIGYF2.

Cinthia C Amaya Ramirez, Petra Hubbe, Nicolas Mandel, Julien Béthune

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
3.1field-weighted citation impact, top 8% 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, 61 citations in OpenAlex.

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  12. SARS-CoV-2 impairs interferon production via NSP2-induced repression of mRNA translation.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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.

Cinthia C Amaya RamirezCellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University, D-69120 Heidelberg, Germany.
Petra HubbeCellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University, D-69120 Heidelberg, Germany.
Nicolas MandelCellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University, D-69120 Heidelberg, Germany.
Julien BéthuneCellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University, D-69120 Heidelberg, Germany.
Heidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Initially identified as a factor involved in tyrosine kinase receptor signaling, Grb10-interacting GYF protein 2 (GIGYF2) has later been shown to interact with the 5' cap-binding protein 4EHP as part of a translation repression complex, and to mediate post-transcriptional repression of tethered reporter mRNAs. A current model proposes that GIGYF2 is indirectly recruited to mRNAs by specific RNA-binding proteins (RBPs) leading to translation repression through its association with 4EHP. Accordingly, we recently observed that GIGYF2 also interacts with the miRNA-induced silencing complex and probably modulates its translation repression activity. Here we have further investigated how GIGYF2 represses mRNA function. In a tethering reporter assay, we identify three independent domains of GIGYF2 with repressive activity. In this assay, GIGYF2-mediated repression is independent of 4EHP but largely dependent on the CCR4/NOT complex that GIGYF2 recruits through multiple interfaces. Importantly, we show that GIGYF2 is an RBP and identify for the first time endogenous mRNA targets that recapitulate 4EHP-independent repression. Altogether, we propose that GIGYF2 has two distinct mechanisms of repression: one depends on 4EHP binding and mainly affects translation; the other is 4EHP-independent and involves the CCR4/NOT complex and its deadenylation activity.

Indexed as

Protein BiosynthesisRNA StabilityCarrier ProteinsEukaryotic Initiation Factor-4EHeLa CellsHumansProtein DomainsRibonucleasesRNA-Binding ProteinsRNA Cap-Binding ProteinsRNA, MessengerCarrier ProteinsEIF4E2 protein, humanEukaryotic Initiation Factor-4EGIGYF2 protein, humanmRNA deadenylaseRibonucleasesRNA-Binding ProteinsRNA Cap-Binding ProteinsRNA, Messenger

Identifiers

PMID29554310
PMCPMC6009589
OpenAlexW2790878015

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.