ArticleRNA (New York, N.Y.)2012
Crystal structure of a minimal eIF4E-Cup complex reveals a general mechanism of eIF4E regulation in translational repression.
Article in RNA (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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.
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.
Who cites it
39 citing papers in PubMed, 64 citations in OpenAlex.
- Cytoplasmic mRNA decay and quality control machineries in eukaryotes.Nature reviews. Genetics · 2025Review
- Review
- Biochemical analysis of human eIF4E-DCP2 interaction: Implications for the relationship between translation initiation and decapping.PloS one · 2025Article
- Exploring the dynamics of messenger ribonucleoprotein-mediated translation repression.Biochemical Society transactions · 2024Review
- Greatwall-Endos-PP2A/B55Open biology · 2024Article
- ReLo is a simple and rapid colocalization assay to identify and characterize direct protein-protein interactions.Nature communications · 2024Article
- C8ORF88: A Novel eIF4E-Binding Protein.Genes · 2023Article
- An intramolecular disulphide bond in human 4E-T affects its binding to eIF4E1a protein.European biophysics journal : EBJ · 2023Article
- RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system.Nucleic acids research · 2023Article
- Cup is essential forRNA biology · 2023Article
- Control of the eIF4E activity: structural insights and pharmacological implications.Cellular and molecular life sciences : CMLS · 2021Review
- Rapid Genomic Evolution Drives the Diversification of Male Reproductive Genes in Dung Beetles.Genome biology and evolution · 2021Article
- The Dynamic Regulation of mRNA Translation and Ribosome Biogenesis During Germ Cell Development and Reproductive Aging.Frontiers in cell and developmental biology · 2021Review
- Computational study on the allosteric mechanism ofComputational and structural biotechnology journal · 2021Article
- Article
- 4E-T-bound mRNAs are stored in a silenced and deadenylated form.Genes & development · 2020Article
- A newly identified Leishmania IF4E-interacting protein, Leish4E-IP2, modulates the activity of cap-binding protein paralogs.Nucleic acids research · 2020Article
- The suppressive cap-binding complex factor 4EIP is required for normal differentiation.Nucleic acids research · 2018Article
- Structural motifs in eIF4G and 4E-BPs modulate their binding to eIF4E to regulate translation initiation in yeast.Nucleic acids research · 2018Article
- Properties of the ternary complex formed by yeast eIF4E, p20 and mRNA.Scientific reports · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cup is an eIF4E-binding protein (4E-BP) that plays a central role in translational regulation of localized mRNAs during early Drosophila development. In particular, Cup is required for repressing translation of the maternally contributed oskar, nanos, and gurken mRNAs, all of which are essential for embryonic body axis determination. Here, we present the 2.8 Å resolution crystal structure of a minimal eIF4E-Cup assembly, consisting of the interacting regions of the two proteins. In the structure, two separate segments of Cup contact two orthogonal faces of eIF4E. The eIF4E-binding consensus motif of Cup (YXXXXLΦ) binds the convex side of eIF4E similarly to the consensus of other eIF4E-binding proteins, such as 4E-BPs and eIF4G. The second, noncanonical, eIF4E-binding site of Cup binds laterally and perpendicularly to the eIF4E β-sheet. Mutations of Cup at this binding site were shown to reduce binding to eIF4E and to promote the destabilization of the associated mRNA. Comparison with the binding mode of eIF4G to eIF4E suggests that Cup and eIF4G binding would be mutually exclusive at both binding sites. This shows how a common molecular surface of eIF4E might recognize different proteins acting at different times in the same pathway. The structure provides insight into the mechanism by which Cup disrupts eIF4E-eIF4G interaction and has broader implications for understanding the role of 4E-BPs in translational regulation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.