Evidence map›Paper›PMID 29178343›Full record

ArticleCancer science2018

PRDM14 directly interacts with heat shock proteins HSP90α and glucose-regulated protein 78.

Chiharu Moriya, Hiroaki Taniguchi, Satoru Nagatoishi, Hisayoshi Igarashi, Kouhei Tsumoto, Kohzoh Imai

Open access · goldAbstract read
In one paragraph

Article in Cancer science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Therapeutic siRNA targeting the cancer cell stemness regulator PRDI-BF1 and RIZ domain zinc finger protein 14.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Multifaceted Role of PRDM Proteins in Human Cancer.International journal of molecular sciences · 2020
    Review
  12. Review
  13. NanoBRET: The Bright Future of Proximity-Based Assays.Frontiers in bioengineering and biotechnology · 2019
    Review
  14. Article
  15. 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 3 institutions in 1 country.

Chiharu MoriyaCenter for Antibody and Vaccine Therapy, Research Hospital, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.ORCID http://orcid.org/0000-0002-0723-4040
Hiroaki TaniguchiCenter for Antibody and Vaccine Therapy, Research Hospital, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Satoru NagatoishiDepartment of Bioengineering, School of Engineering, The University of Tokyo, Tokyo, Japan.
Hisayoshi IgarashiCenter for Antibody and Vaccine Therapy, Research Hospital, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Kouhei TsumotoDepartment of Bioengineering, School of Engineering, The University of Tokyo, Tokyo, Japan.
Kohzoh ImaiThe Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
University of Tokyo Hospital · JPThe University of Tokyo · JPTokyo Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PRDM14 is overexpressed in various cancers and can regulate cancer phenotype under certain conditions. Inhibiting PRDM14 expression in breast and pancreatic cancers has been reported to reduce cancer stem-like phenotypes, which are associated with aggressive tumor properties. Therefore, PRDM14 is considered a promising target for cancer therapy. To develop a pharmaceutical treatment, the mechanism and interacting partners of PRDM14 need to be clarified. Here, we identified the proteins interacting with PRDM14 in triple-negative breast cancer (TNBC) cells, which do not express the three most common types of receptor (estrogen receptors, progesterone receptors, and HER2). We obtained 13 candidates that were pulled down with PRDM14 in TNBC HCC1937 cells and identified them by mass spectrometry. Two candidates-glucose-regulated protein 78 (GRP78) and heat shock protein 90-α (HSP90α)-were confirmed in immunoprecipitation assay in two TNBC cell lines (HCC1937 and MDA-MB231). Surface plasmon resonance analysis using GST-PRDM14 showed that these two proteins directly interacted with PRDM14 and that the interactions required the C-terminal region of PRDM14, which includes zinc finger motifs. We also confirmed the interactions in living cells by NanoLuc luciferase-based bioluminescence resonance energy transfer (NanoBRET) assay. Moreover, HSP90 inhibitors (17DMAG and HSP990) significantly decreased breast cancer stem-like CD24

Indexed as

Cell Line, TumorCell ProliferationDNA-Binding ProteinsEndoplasmic Reticulum Chaperone BiPFemaleGene Expression Regulation, NeoplasticHeat-Shock ProteinsHEK293 CellsHSP90 Heat-Shock ProteinsHumansMass SpectrometryProtein DomainsProtein Interaction MappingRepressor ProteinsRNA-Binding ProteinsSurface Plasmon ResonanceDNA-Binding ProteinsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSP90AA2P protein, humanHSP90 Heat-Shock ProteinsHSPA5 protein, humanPRDM14 protein, humanRepressor ProteinsRNA-Binding ProteinsTranscription FactorsGRP78heat shock proteinHSP90αPRDM14protein-protein interaction

Identifiers

PMID29178343
PMCPMC5797828
OpenAlexW2768554744

What OpenQuestion holds

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LicenceCC BY-NC
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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.