Evidence map›Paper›PMID 24799437›Full record

ArticleNucleic acids research2014

Staufen1-mediated mRNA decay induces Requiem mRNA decay through binding of Staufen1 to the Requiem 3'UTR.

Min Young Kim, Jungyun Park, Jong Joo Lee, Dae Hyun Ha, Jonghwan Kim, Chan Gil Kim, Jungwook Hwang, Chul Geun Kim

Erratum issuedOpen 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. An erratum has been issued. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

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  11. Histone-binding of DPF2 mediates its repressive role in myeloid differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2017
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Min Young KimDepartment of Life Science and Research Institute for Natural Sciences, College of Natural Sciences.
Jungyun ParkGraduate School for Biomedical Science and Engineering, Hanyang University, Seoul 133-791, Korea.
Jong Joo LeeDepartment of Life Science and Research Institute for Natural Sciences, College of Natural Sciences.
Dae Hyun HaDepartment of Life Science and Research Institute for Natural Sciences, College of Natural Sciences.
Jonghwan KimDepartment of Life Science and Research Institute for Natural Sciences, College of Natural Sciences.
Chan Gil KimDepartment of Biotechnology, Konkuk University, Chungju 380-701, Korea.
Jungwook HwangGraduate School for Biomedical Science and Engineering, Hanyang University, Seoul 133-791, Korea jwhwang@hanyang.ac.kr.
Chul Geun KimDepartment of Life Science and Research Institute for Natural Sciences, College of Natural Sciences cgkim@hanyang.ac.kr.
Institute of Natural Science · KPHanyang University · KRKonkuk University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Requiem (REQ/DPF2) was originally identified as an apoptosis-inducing protein in mouse myeloid cells and belongs to the novel Krüppel-type zinc finger d4-protein family of proteins, which includes neuro-d4 (DPF1) and cer-d4 (DPF3). Interestingly, when a portion of the REQ messenger ribonucleic acid (mRNA) 3' untranslated region (3'UTR), referred to as G8, was overexpressed in K562 cells, β-globin expression was induced, suggesting that the 3'UTR of REQ mRNA plays a physiological role. Here, we present evidence that the REQ mRNA 3'UTR, along with its trans-acting factor, Staufen1 (STAU1), is able to reduce the level of REQ mRNA via STAU1-mediated mRNA decay (SMD). By screening a complementary deoxyribonucleic acid (cDNA) expression library with an RNA-ligand binding assay, we identified STAU1 as an interactor of the REQ mRNA 3'UTR. Specifically, we provide evidence that STAU1 binds to putative 30-nucleotide stem-loop-structured RNA sequences within the G8 region, which we term the protein binding site core; this binding triggers the degradation of REQ mRNA and thus regulates translation. Furthermore, we demonstrate that siRNA-mediated silencing of either STAU1 or UPF1 increases the abundance of cellular REQ mRNA and, consequently, the REQ protein, indicating that REQ mRNA is a target of SMD.

Indexed as

3' Untranslated RegionsRNA StabilityAnimalsBinding SitesCell LineCytoskeletal ProteinsDNA-Binding ProteinsHeLa CellsHumansK562 CellsMiceNucleic Acid ConformationRNA-Binding ProteinsRNA, MessengerTranscription Factors3' Untranslated RegionsCytoskeletal ProteinsDNA-Binding ProteinsDPF2 protein, humanRNA-Binding ProteinsRNA, MessengerSTAU1 protein, humanTranscription Factors

Identifiers

PMID24799437
PMCPMC4066795
OpenAlexW2166195235

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.