Evidence map›Paper›PMID 40908296›Full record

ArticleBritish journal of cancer2025

Inhibition of YB-1 phosphorylation enhances cisplatin activity and disrupts cell division in pleural mesothelioma.

Karin Schelch, Nadine Maach, Muhammad Hashim, Benjamin Zitta, Dominik Kirchhofer, Gerald Timelthaler, Anna Solta, Dominik Emminger, Verena Kopatz, Mir A Hoda and 5 more

Abstract read
In one paragraph

Article in British journal of cancer, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

15 authors.

Karin SchelchCenter for Cancer Research, Medical University of Vienna, Vienna, Austria.ORCID http://orcid.org/0000-0001-8742-1737
Nadine MaachCenter for Cancer Research, Medical University of Vienna, Vienna, Austria.
Muhammad HashimCenter for Cancer Research, Medical University of Vienna, Vienna, Austria.
Benjamin ZittaCenter for Cancer Research, Medical University of Vienna, Vienna, Austria.
Dominik KirchhoferCenter for Cancer Research, Medical University of Vienna, Vienna, Austria.
Gerald TimelthalerCenter for Cancer Research, Medical University of Vienna, Vienna, Austria.
Anna SoltaDepartment of Thoracic Surgery, Medical University of Vienna, Vienna, Austria.
Dominik EmmingerCenter for Cancer Research, Medical University of Vienna, Vienna, Austria.
Verena KopatzDepartment of Radiation Oncology, Applied and Translational Radiobiology, Medical University of Vienna, Vienna, Austria.ORCID http://orcid.org/0000-0002-7512-1398
Mir A HodaDepartment of Thoracic Surgery, Medical University of Vienna, Vienna, Austria.
Walter BergerCenter for Cancer Research, Medical University of Vienna, Vienna, Austria.ORCID http://orcid.org/0000-0003-0014-1658
Clemens AignerDepartment of Thoracic Surgery, Medical University of Vienna, Vienna, Austria.ORCID http://orcid.org/0000-0002-7787-991X
Balazs DomeDepartment of Thoracic Surgery, Medical University of Vienna, Vienna, Austria.ORCID http://orcid.org/0000-0001-8799-8624
Glen ReidDepartment of Pathology, Dunedin School of Medicine, Dunedin, New Zealand.
Michael GruschCenter for Cancer Research, Medical University of Vienna, Vienna, Austria. michael.grusch@meduniwien.ac.at.ORCID http://orcid.org/0000-0001-5486-9340

Funding

Austrian Science Fund (Fonds zur Förderung der Wissenschaftlichen Forschung) T 1062-B33
6 · The paper itself

Abstract

backgroundThe cold-shock domain protein YB-1 is overexpressed in pleural mesothelioma (PM) and was shown to contribute to increased cell migration and platinum resistance.

methodsPhosphorylation of YB-1 at position serine 102 was analysed by immunohistochemistry, immunofluorescence and immunoblotting in PM tissue specimens and cell lines. Intracellular localisation experiments involved immunoblotting, transfection of fluorescent protein-tagged YB-1 and confocal imaging. YB-1 phosphorylation was inhibited with the RSK inhibitors BI-D1870 and LJH685. Effects of inhibition alone and in combination with radiation or cisplatin treatment were analysed by cell viability assays, clonogenic assays and videomicroscopy-based migration and cell fate map analyses.

resultsYB-1 phosphorylated at serine 102 is present in PM cell lines and tissue. Inhibition of phosphorylation with BI-D1870 reduced YB-1 localisation in the cell nucleus and led to reduced cell viability, clonogenicity, migration and disrupted cell division. Moreover, exposure to BI-D1870 increased the effect of radiation and cisplatin treatment with additive to synergistic effects in PM cell lines and primary cultures.

conclusionsThe serine 102 phosphorylated form of YB-1 contributes to the malignant phenotype of PM. Inhibition of YB-1 phosphorylation warrants further exploration as part of treatment strategies for this devastating disease.

Indexed as

Antineoplastic AgentsCisplatinMesotheliomaPleural NeoplasmsY-Box-Binding Protein 1Cell DivisionCell Line, TumorCell MovementCell SurvivalHumansMesothelioma, MalignantPhosphorylationAntineoplastic AgentsCisplatinY-Box-Binding Protein 1YBX1 protein, human

Identifiers

PMID40908296
PMCPMC12572334

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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.