Evidence map›Paper›PMID 25016523›Full record

ArticleNucleic acids research2014

The mRNP remodeling mediated by UPF1 promotes rapid degradation of replication-dependent histone mRNA.

Junho Choe, Sang Ho Ahn, Yoon Ki Kim

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

28 citing papers in PubMed, 39 citations in OpenAlex.

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  9. Tailor made: the art of therapeutic mRNA design.Nature reviews. Drug discovery · 2024
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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

3 authors at 1 institution in 1 country.

Junho ChoeDivision of Life Sciences, Korea University, Seoul 136-701, Republic of Korea.
Sang Ho AhnDivision 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 · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone biogenesis is tightly controlled at multiple steps to maintain the balance between the amounts of DNA and histone protein during the cell cycle. In particular, translation and degradation of replication-dependent histone mRNAs are coordinately regulated. However, the underlying molecular mechanisms remain elusive. Here, we investigate remodeling of stem-loop binding protein (SLBP)-containing histone mRNPs occurring during the switch from the actively translating mode to the degradation mode. The interaction between a CBP80/20-dependent translation initiation factor (CTIF) and SLBP, which is important for efficient histone mRNA translation, is disrupted upon the inhibition of DNA replication or at the end of S phase. This disruption is mediated by competition between CTIF and UPF1 for SLBP binding. Further characterizations reveal hyperphosphorylation of UPF1 by activated ATR and DNA-dependent protein kinase upon the inhibition of DNA replication interacts with SLBP more strongly, promoting the release of CTIF and eIF3 from SLBP-containing histone mRNP. In addition, hyperphosphorylated UPF1 recruits PNRC2 and SMG5, triggering decapping followed by 5'-to-3' degradation of histone mRNAs. The collective observations suggest that both inhibition of translation and recruitment of mRNA degradation machinery during histone mRNA degradation are tightly coupled and coordinately regulated by UPF1 phosphorylation.

Indexed as

DNA ReplicationRNA Stability3' Untranslated RegionsAtaxia Telangiectasia Mutated ProteinsDNA-Activated Protein KinaseEukaryotic Initiation FactorsHEK293 CellsHeLa CellsHistonesHumansmRNA Cleavage and Polyadenylation FactorsNuclear ProteinsPhosphorylationRibonucleoproteinsRNA HelicasesRNA, Messenger3' Untranslated RegionsAtaxia Telangiectasia Mutated ProteinsATR protein, humanCTIF protein, humanDNA-Activated Protein KinaseEukaryotic Initiation FactorsHistonesmessenger ribonucleoproteinmRNA Cleavage and Polyadenylation FactorsNuclear ProteinsRibonucleoproteinsRNA HelicasesRNA, MessengerSLBP protein, humanTrans-ActivatorsUPF1 protein, human

Identifiers

PMID25016523
PMCPMC4132728
OpenAlexW2058701584

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.