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This study investigates the role of dual\u2010specificity phosphatase 12 (DUSP12) and its interaction with the nucleolar protein\n                    <jats:italic>N<\/jats:italic>\n                    \u2010acetyltransferase 10 (NAT10) in HCC models under genotoxic stress. We demonstrate that doxorubicin (DX) induces greater cytotoxicity than cisplatin, correlating with a stronger DNA damage response (DDR), nucleolar stress, and NAT10 relocalization. CRISPR\u2010Cas9\u2010mediated DUSP12 knockout sensitized cells to DX, increasing markers of DNA damage (\u03b3H2AX, p53) and delaying DNA break repair. This was accompanied by redistribution of nucleolar proteins NAT10 and TCOF1. Remodelin treatment enhanced DX sensitivity in DUSP12 knockout cells, suggesting a context\u2010dependent interaction between DUSP12 loss and the NAT10 inhibition. Protein interaction assays confirmed that DUSP12 binds NAT10, corroborating a regulatory interaction. 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Our findings identify the DUSP12\u2013NAT10\u2013ac4C axis as a novel molecular link between DDR and nucleolar stress, unveiling a potential therapeutic vulnerability in HCC.\n                  <\/jats:p>","DOI":"10.1002\/mco2.70929","type":"journal-article","created":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T06:55:04Z","timestamp":1787036104000},"source":"Crossref","is-referenced-by-count":0,"title":["DUSP12 Regulates NAT10\u2010Mediated RNA Acetylation to Modulate DNA Repair and Therapeutic Response in Hepatocellular Carcinoma"],"prefix":"10.1002","volume":"7","author":[{"given":"Viktor Kalbermatter","family":"Boell","sequence":"first","affiliation":[{"name":"Department of Biochemistry Institute of Chemistry University of S\u00e3o Paulo (USP)  S\u00e3o Paulo Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Diana Reis Della Corte Guimar\u00e3es","family":"Pacheco","sequence":"additional","affiliation":[{"name":"Department of Biochemistry Institute of 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