Evidence map›Paper›PMID 31114929›Full record

ArticleNucleic acids research2019

Direct role for the Drosophila GIGYF protein in 4EHP-mediated mRNA repression.

Vincenzo Ruscica, Praveen Bawankar, Daniel Peter, Sigrun Helms, Cátia Igreja, Elisa Izaurralde

Open access · goldAbstract readComparative Study
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

18 citing papers in PubMed, 43 citations in OpenAlex.

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  5. The role of m5C, m1A and m7G modifications in tumors of urinary system.Frontiers in cell and developmental biology · 2025
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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

6 authors at 1 institution in 2 countries.

Vincenzo RuscicaDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Max-Planck-Ring 5, D-72076 Tübingen, Germany.
Praveen BawankarDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Max-Planck-Ring 5, D-72076 Tübingen, Germany.
Daniel PeterDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Max-Planck-Ring 5, D-72076 Tübingen, Germany.
Sigrun HelmsDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Max-Planck-Ring 5, D-72076 Tübingen, Germany.
Cátia IgrejaDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Max-Planck-Ring 5, D-72076 Tübingen, Germany.
Elisa IzaurraldeDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Max-Planck-Ring 5, D-72076 Tübingen, Germany.
Max Planck Institute for Developmental Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The eIF4E-homologous protein (4EHP) is a translational repressor that competes with eIF4E for binding to the 5'-cap structure of specific mRNAs, to which it is recruited by protein factors such as the GRB10-interacting GYF (glycine-tyrosine-phenylalanine domain) proteins (GIGYF). Several experimental evidences suggest that GIGYF proteins are not merely facilitating 4EHP recruitment to transcripts but are actually required for the repressor activity of the complex. However, the underlying molecular mechanism is unknown. Here, we investigated the role of the uncharacterized Drosophila melanogaster (Dm) GIGYF protein in post-transcriptional mRNA regulation. We show that, when in complex with 4EHP, Dm GIGYF not only elicits translational repression but also promotes target mRNA decay via the recruitment of additional effector proteins. We identified the RNA helicase Me31B/DDX6, the decapping activator HPat and the CCR4-NOT deadenylase complex as binding partners of GIGYF proteins. Recruitment of Me31B and HPat via discrete binding motifs conserved among metazoan GIGYF proteins is required for downregulation of mRNA expression by the 4EHP-GIGYF complex. Our findings are consistent with a model in which GIGYF proteins additionally recruit decapping and deadenylation complexes to 4EHP-containing RNPs to induce translational repression and degradation of mRNA targets.

Indexed as

Gene Expression RegulationAmino Acid SequenceAnimalsConserved SequenceDEAD-box RNA HelicasesDown-RegulationDrosophila melanogasterDrosophila ProteinsEndopeptidasesEukaryotic Initiation Factor-4EGenes, ReporterMultiprotein ComplexesProtein BiosynthesisRepressor ProteinsRibonucleasesRNA-Binding ProteinsCCR4 protein, DrosophilaDEAD-box RNA HelicasesDrosophila ProteinseIF4EHP protein, DrosophilaEndopeptidasesEukaryotic Initiation Factor-4EGyf protein, DrosophilaMe31B protein, DrosophilaMultiprotein Complexesnot protein, DrosophilaPatr-1 protein, DrosophilaRepressor ProteinsRibonucleasesRNA-Binding ProteinsRNA Cap-Binding ProteinsRNA CapsRNA, Messenger

Identifiers

PMID31114929
PMCPMC6648886
OpenAlexW2945365446

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.