ArticleChemical research in toxicology2020
Arsenite Binds to ZNF598 to Perturb Ribosome-Associated Protein Quality Control.
Article in Chemical research in toxicology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Arsenic regulates ALKBH1 abundance and substrate specificity to promote translation and tumorigenicity.Cell reports · 2025Article
- Epitranscriptomic alterations induced by environmental toxins: implications for RNA modifications and disease.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2025Review
- PRDX1 protects ATM from arsenite-induced proteotoxicity and maintains its stability during DNA damage signaling.Oncotarget · 2025Article
- Chemoproteomic Approach for Identifying Nuclear Arsenite-Binding Proteins.Chemical research in toxicology · 2025Article
- Dysregulated ribosome quality control in human diseases.The FEBS journal · 2025Review
- Mechanistic understanding of the toxic effects of arsenic and warfare arsenicals on human health and environment.Cell biology and toxicology · 2023Review
- Chemoproteomic Approach for the Quantitative Identification of Arsenic-Binding Proteins.Chemical research in toxicology · 2022Article
- Quantitative Assessment of Arsenite-Induced Perturbation of Ubiquitinated Proteome.Chemical research in toxicology · 2022Article
- Arsenic Exposure and Compromised Protein Quality Control.Chemical research in toxicology · 2020Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Arsenic pollution in drinking water is a widespread public health problem, and it affects approximately 200 million people in over 70 countries. Many human diseases, including neurodegenerative disorders, are engendered by the malfunction of proteins involved in important biological processes and are elicited by protein misfolding and/or loss of protein quality control during translation. Arsenic exposure results in proteotoxic stress, though the detailed molecular mechanisms remain poorly understood. Here, we showed that arsenite interacts with ZNF598 protein in cells and exposure of human skin fibroblasts to arsenite results in significant decreases in the ubiquitination levels of lysine residues 138 and 139 in RPS10 and lysine 8 in RPS20, which are regulatory post-translational modifications important in ribosome-associated protein quality control. Furthermore, the arsenite-elicited diminutions in ubiquitinations of RPS10 and RPS20 gave rise to augmented read-through of poly(adenosine)-containing stalling sequences, which was abolished in ZNF598 knockout cells. Together, our study revealed a novel mechanism underlying the arsenic-induced proteostatic stress in human cells.
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Registered trials
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