Evidence map›Paper›PMID 25313076›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

eIF4AIII enhances translation of nuclear cap-binding complex-bound mRNAs by promoting disruption of secondary structures in 5'UTR.

Junho Choe, Incheol Ryu, Ok Hyun Park, Joori Park, Hana Cho, Jin Seon Yoo, Sung Wook Chi, Min Kyung Kim, Hyun Kyu Song, Yoon Ki Kim

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. 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
2.7field-weighted citation impact, top 9% 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

45 citing papers in PubMed, 70 citations in OpenAlex.

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  4. Gene regulation through exon junction complex modularity.Nature structural & molecular 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

10 authors at 3 institutions in 1 country.

Junho ChoeDivision of Life Sciences, Korea University, Seoul 136-701, Republic of Korea;
Incheol RyuDivision of Life Sciences, Korea University, Seoul 136-701, Republic of Korea;
Ok Hyun ParkDivision of Life Sciences, Korea University, Seoul 136-701, Republic of Korea;
Joori ParkDivision of Life Sciences, Korea University, Seoul 136-701, Republic of Korea;
Hana ChoDivision of Life Sciences, Korea University, Seoul 136-701, Republic of Korea;
Jin Seon YooDepartment of Health Sciences and Technology, Samsung Advanced Institute for Health Sciences and Technology, Sungkyunkwan University, Seoul 135-710, Republic of Korea; and.
Sung Wook ChiDepartment of Health Sciences and Technology, Samsung Advanced Institute for Health Sciences and Technology, Sungkyunkwan University, Seoul 135-710, Republic of Korea; and Samsung Research Institute for Future Medicine, Samsung Medical Center, Seoul 135-710, Republic of Korea.
Min Kyung KimDivision of Life Sciences, Korea University, Seoul 136-701, Republic of Korea;
Hyun Kyu SongDivision of Life Sciences, Korea University, Seoul 136-701, Republic of Korea;
Yoon Ki KimDivision of Life Sciences, Korea University, Seoul 136-701, Republic of Korea; yk-kim@korea.ac.kr.
Korea University · KRSamsung (South Korea) · KRSungkyunkwan University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It has long been considered that intron-containing (spliced) mRNAs are translationally more active than intronless mRNAs (identical mRNA not produced by splicing). The splicing-dependent translational enhancement is mediated, in part, by the exon junction complex (EJC). Nonetheless, the molecular mechanism by which each EJC component contributes to the translational enhancement remains unclear. Here, we demonstrate the previously unappreciated role of eukaryotic translation initiation factor 4AIII (eIF4AIII), a component of EJC, in the translation of mRNAs bound by the nuclear cap-binding complex (CBC), a heterodimer of cap-binding protein 80 (CBP80) and CBP20. eIF4AIII is recruited to the 5'-end of mRNAs bound by the CBC by direct interaction with the CBC-dependent translation initiation factor (CTIF); this recruitment of eIF4AIII is independent of the presence of introns (deposited EJCs after splicing). Polysome fractionation, tethering experiments, and in vitro reconstitution experiments using recombinant proteins show that eIF4AIII promotes efficient unwinding of secondary structures in 5'UTR, and consequently enhances CBC-dependent translation in vivo and in vitro. Therefore, our data provide evidence that eIF4AIII is a specific translation initiation factor for CBC-dependent translation.

Indexed as

Nucleic Acid ConformationProtein Biosynthesis5' Untranslated RegionsCell NucleusDNA ReplicationDown-RegulationEukaryotic Initiation Factor-4AEukaryotic Initiation FactorsHEK293 CellsHeLa CellsHistonesHumansIntronsModels, BiologicalProtein BindingRecombinant Proteins5' Untranslated RegionsCTIF protein, humanEukaryotic Initiation Factor-4AEukaryotic Initiation FactorsHistonesRecombinant ProteinsRNA CapsRNA, Messengercap-binding complexCTIFeIF4AIIInonsense-mediated mRNA decaytranslation

Identifiers

PMID25313076
PMCPMC4217471
OpenAlexW2076494516

What OpenQuestion holds

Textmetadata
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.