Evidence map›Paper›PMID 28698298›Full record

ArticleGenes & development2017

GIGYF1/2 proteins use auxiliary sequences to selectively bind to 4EHP and repress target mRNA expression.

Daniel Peter, Ramona Weber, Felix Sandmeir, Lara Wohlbold, Sigrun Helms, Praveen Bawankar, Eugene Valkov, Cátia Igreja, Elisa Izaurralde

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
–field-weighted citation impact
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

45 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. The role of m5C, m1A and m7G modifications in tumors of urinary system.Frontiers in cell and developmental biology · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Construction of a Diagnostic mBiomolecules · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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
    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

9 authors at 1 institution in 1 country.

Daniel PeterDepartment of Biochemistry, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany.
Ramona WeberDepartment of Biochemistry, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany.
Felix SandmeirDepartment of Biochemistry, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany.
Lara WohlboldDepartment of Biochemistry, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany.
Sigrun HelmsDepartment of Biochemistry, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany.
Praveen BawankarDepartment of Biochemistry, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany.
Eugene ValkovDepartment of Biochemistry, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany.
Cátia IgrejaDepartment of Biochemistry, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany.
Elisa IzaurraldeDepartment of Biochemistry, Max Planck Institute for Developmental Biology, 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 thought to repress translation by competing with eIF4E for binding to the 5' cap structure of specific mRNAs to which it is recruited through interactions with various proteins, including the GRB10-interacting GYF (glycine-tyrosine-phenylalanine domain) proteins 1 and 2 (GIGYF1/2). Despite its similarity to eIF4E, 4EHP does not interact with eIF4G and therefore fails to initiate translation. In contrast to eIF4G, GIGYF1/2 bind selectively to 4EHP but not eIF4E. Here, we present crystal structures of the 4EHP-binding regions of GIGYF1 and GIGYF2 in complex with 4EHP, which reveal the molecular basis for the selectivity of the GIGYF1/2 proteins for 4EHP. Complementation assays in a GIGYF1/2-null cell line using structure-based mutants indicate that 4EHP requires interactions with GIGYF1/2 to down-regulate target mRNA expression. Our studies provide structural insights into the assembly of 4EHP-GIGYF1/2 repressor complexes and reveal that rather than merely facilitating 4EHP recruitment to transcripts, GIGYF1/2 proteins are required for repressive activity.

Indexed as

Carrier ProteinsCell LineCrystallizationEukaryotic Initiation Factor-4EGene Expression RegulationHEK293 CellsHumansModels, MolecularMutationProtein BindingProtein StabilityProtein Structure, QuaternaryRNA Cap-Binding ProteinsRNA, MessengerCarrier ProteinsEIF4E2 protein, humanEukaryotic Initiation Factor-4EGIGYF1 protein, humanGIGYF2 protein, humanRNA Cap-Binding ProteinsRNA, MessengereIF4Etranslational regulationtranslational repression

Identifiers

PMID28698298
PMCPMC5538437
OpenAlexW2735357942

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.