Evidence map›Paper›PMID 12192037›Full record

ArticleMolecular and cellular biology2002

Novel translational control through an iron-responsive element by interaction of multifunctional protein YB-1 and IRP2.

Megumi Ashizuka, Takao Fukuda, Takanori Nakamura, Kanemitsu Shirasuna, Kazuhiro Iwai, Hiroto Izumi, Kimitoshi Kohno, Michihiko Kuwano, Takeshi Uchiumi

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. 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
1.3field-weighted citation impact, top 21% 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, 62 citations in OpenAlex.

  1. Article
  2. Review
  3. The Pleiotropic Effects of YBX1 on HTLV-1 Transcription.International journal of molecular sciences · 2023
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  7. Review
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  15. Regulation of zinc-responsive Slc39a5 (Zip5) translation is mediated by conserved elements in the 3'-untranslated region.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2012
    Article
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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

9 authors at 4 institutions in 1 country.

Megumi AshizukaDepartment of Medical Biochemistry, Graduate School of Medical Sciences, Kyushu University, Higashi-ku, Fukuoka 812-8582, Japan.
Takao Fukuda
Takanori Nakamura
Kanemitsu Shirasuna
Kazuhiro Iwai
Hiroto Izumi
Kimitoshi Kohno
Michihiko Kuwano
Takeshi Uchiumi
Kumamoto University · JPKyushu University · JPUniversity of Occupational and Environmental Health Japan · JPOsaka City University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The eukaryotic Y-box-binding protein YB-1 functions in various biological processes, including DNA repair, cell proliferation, and transcriptional and translational controls. To gain further insight into how human YB-1 plays its role in pleiotropic functions, we here used two-hybrid screenings to identify partners of this protein; the results showed that YB-1 itself, iron-regulatory protein 2 (IRP2), and five ribosomal proteins each served as partners to YB-1. We then examined the biological effect of the interaction of YB-1 and IRP2 on translational regulation. Both in vitro binding and coimmunoprecipitation assays showed the direct interaction of YB-1 and IRP2 in the presence of a high concentration of iron. RNA gel shift assays showed that YB-1 reduced the formation of the IRP2-mRNA complex when the iron-responsive element of the ferritin mRNA 5' untranslated region (UTR) was used as a probe. By using an in vitro translation assay using luciferase mRNA ligated to the ferritin mRNA 5'UTR as a reporter construct, we showed that both YB-1 and IRP2 inhibited the translation of the mRNA. However, coadministration of YB-1 and IRP2 proteins abrogated the inhibition of protein synthesis by each protein. An In vivo coimmunoprecipitation assay showed that IRP2 bound to YB-1 in the presence of iron and a proteasome inhibitor. The direct interaction of YB-1 and IRP2 provides the first evidence of the involvement of YB-1 in the translational regulation of an iron-related protein.

Indexed as

DNA-Binding ProteinsProtein BiosynthesisTranscription Factors5' Untranslated RegionsAnimalsCCAAT-Enhancer-Binding ProteinsCell DivisionCell LineDNA RepairDose-Response Relationship, DrugFerritinsGene Expression RegulationGlutathione TransferaseIronIron Regulatory Protein 2Iron-Regulatory Proteins5' Untranslated RegionsCCAAT-Enhancer-Binding ProteinsDNA-Binding ProteinsFerritinsGlutathione TransferaseIronIron Regulatory Protein 2Iron-Regulatory ProteinsIron-Sulfur ProteinsNFI Transcription FactorsNuclear ProteinsRNA-Binding ProteinsRNA, MessengerTranscription FactorsY-Box-Binding Protein 1YBX1 protein, human

Identifiers

PMID12192037
PMCPMC135634
OpenAlexW2160476153

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.