Evidence map›Paper›PMID 29670170›Full record

ArticleScientific reports2018

Y-box protein-associated acidic protein (YBAP1/C1QBP) affects the localization and cytoplasmic functions of YB-1.

Ken Matsumoto, Shingo Kose, Iku Kuwahara, Mami Yoshimura, Naoko Imamoto, Minoru Yoshida

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. YB1 and its role in osteosarcoma: a review.Frontiers in oncology · 2024
    Review
  3. Article
  4. Article
  5. YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation.International journal of molecular sciences · 2021
    Article
  6. Elucidating the molecular signaling pathways of WAVE3.Annals of translational medicine · 2020
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
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

6 authors at 4 institutions in 1 country.

Ken MatsumotoChemical Genomics Research Group, RIKEN Center for Sustainable Resource Science, RIKEN, Wako, Saitama, Japan. matsumok@riken.jp.ORCID 0000-0002-7864-3394
Shingo KoseCellular Dynamics Laboratory, RIKEN Cluster for Pioneering Research (CPR), RIKEN, Wako, Saitama, Japan.
Iku KuwaharaMolecular Entomology Laboratory, RIKEN, Wako, Saitama, Japan.
Mami YoshimuraMolecular Entomology Laboratory, RIKEN, Wako, Saitama, Japan.
Naoko ImamotoCellular Dynamics Laboratory, RIKEN Cluster for Pioneering Research (CPR), RIKEN, Wako, Saitama, Japan.
Minoru YoshidaChemical Genomics Research Group, RIKEN Center for Sustainable Resource Science, RIKEN, Wako, Saitama, Japan.
Pioneer (Japan) · JPRIKEN · JPJapan Science and Technology Agency · JPRIKEN Center for Sustainable Resource Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Y-box proteins are multifunctional nucleic acid-binding proteins involved in various aspects of gene regulation. The founding member of the Y-box protein family, YB-1, functions as a transcription factor as well as a principal component of messenger ribonucleoprotein particles (mRNPs) in somatic cells. The nuclear level of YB-1 is well correlated with poor prognosis in many human cancers. Previously, we showed that a Y-box protein-associated acidic protein, YBAP1, which is identical to complement component 1, q subcomponent-binding protein (C1QBP, also called gC1qR, hyaluronan-binding protein 1 [HABP1] or ASF/SF2-associated protein p32), relieves translational repression by YB-1. Here we show that the nuclear localization of YB-1 harboring a point mutation in the cold shock domain was inhibited when co-expressed with YBAP1, whereas cytoplasmic accumulation of the wild-type YB-1 was not affected. We showed that YBAP1 inhibited the interaction between YB-1 and transportin 1. In the cytoplasm, YBAP1 affected the accumulation of YB-1 to processing bodies (P-bodies) and partially abrogated the mRNA stabilization by YB-1. Our results, indicating that YBAP1/C1QBP regulates the nucleo-cytoplasmic distribution of YB-1 and its cytoplasmic functions, are consistent with a model that YBAP1/C1QBP acts as an mRNP remodeling factor.

Indexed as

beta KaryopherinsCarrier ProteinsCell NucleusCytoplasmGene ExpressionHeLa CellsHumansMitochondrial ProteinsModels, BiologicalMutationProtein BindingProtein Interaction Domains and MotifsProtein TransportRNA, MessengerRNA StabilityY-Box-Binding Protein 1beta KaryopherinsC1QBP protein, humanCarrier ProteinsMitochondrial ProteinsRNA, MessengerTNPO1 protein, humanY-Box-Binding Protein 1

Identifiers

PMID29670170
PMCPMC5906478
OpenAlexW2802335644

What OpenQuestion holds

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Registered trials

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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.