Evidence map›Paper›PMID 40717513›Full record

ArticleJournal of cell science2025

Arsenic binds to nuclear transport factors and disrupts nucleocytoplasmic transport.

Emma Lorentzon, Jongmin Lee, Jakub Masaryk, Katharina Keuenhof, Nora Karlsson, Charlotte Galipaud, Rebecca Madsen, Johanna L Höög, David E Levin, Markus J Tamás

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of cell science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Emma LorentzonDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 462, S-405 30 Göteborg, Sweden.
Jongmin LeeDepartment of Molecular and Cell Biology, Boston University Henry M. Goldman School of Dental Medicine, Boston, MA 02118, USA.
Jakub MasarykDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 462, S-405 30 Göteborg, Sweden.
Katharina KeuenhofDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 462, S-405 30 Göteborg, Sweden.
Nora KarlssonDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 462, S-405 30 Göteborg, Sweden.
Charlotte GalipaudDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 462, S-405 30 Göteborg, Sweden.
Rebecca MadsenDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 462, S-405 30 Göteborg, Sweden.
Johanna L HöögDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 462, S-405 30 Göteborg, Sweden.ORCID 0000-0003-2162-3816
David E LevinDepartment of Molecular and Cell Biology, Boston University Henry M. Goldman School of Dental Medicine, Boston, MA 02118, USA.ORCID 0000-0003-0696-2860
Markus J TamásDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 462, S-405 30 Göteborg, Sweden.ORCID 0000-0002-0762-7848

Funding

ROLE OF PROTEIN KINASE C IN YEAST GROWTH CONTROLR01GM048533 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI LEVIN, DAVID E. · 1992 to 2025
$7.8M
The Arsenic Stress Signaling Code of YeastR01GM138413 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LEVIN, DAVID E. · 2020 to 2023
$1.8M
Cancerfonden 211-865NIGMS NIH HHS R01 GM048533NIGMS NIH HHS R01 GM138413NIH HHS R01GM138413NIH HHS R01GM48533Olle Engkvists Stiftelse 216-0452Stiftelsen Bengt Lundqvists MinneSven och Dagmar Saléns StiftelseUniversity of GothenburgVetenskapsrådet 2018-03577Vetenskapsrådet 2019-4004
6 · The paper itself

Abstract

Human exposure to arsenicals is associated with devastating diseases such as cancer and neurodegeneration. At the same time, arsenic-based drugs are used as therapeutic agents. The ability of arsenic to directly bind to proteins is correlated with its toxic and therapeutic effects, highlighting the importance of elucidating arsenic-protein interactions. In this study, we took a proteomic approach and identified 174 proteins that bind to arsenic in Saccharomyces cerevisiae. Proteins involved in nucleocytoplasmic transport were markedly enriched among the arsenic-binding proteins, and we demonstrate that arsenic binding to nuclear import factors results in their relocation from the nuclear envelope and subsequent aggregation in the cytosol. Similarly, nuclear pore proteins that make up the nuclear pore complex mislocalized and aggregated in arsenic-exposed cells. Consequently, arsenic was shown to inhibit nuclear protein import and export. We propose a model in which arsenic binding to nuclear transport factors leads to their mislocalization and aggregation, which disrupts nucleocytoplasmic transport and causes arsenic sensitivity.

Indexed as

Active Transport, Cell NucleusArsenicCell NucleusSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHumansNuclear EnvelopeNuclear PoreNuclear Pore Complex ProteinsProtein BindingArsenicNuclear Pore Complex ProteinsSaccharomyces cerevisiae ProteinsArsenicKaryopherinNuclear envelopeNuclear exportNuclear importNuclear pore complexNuclear pore protein

Identifiers

PMID40717513
PMCPMC12401540

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.