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While ATM kinase is traditionally recognized as the primary mediator of H2A.X phosphorylation, our study identifies serine\/threonine kinase 39 (STK39) as a novel enhancer of this critical signaling pathway. We demonstrate that after DNA damage, STK39 undergoes phosphorylation by the ATM kinase, facilitating its interaction with the Mre11-Rad50-Nbs1 complex and subsequent recruitment to chromatin. This recruitment enables STK39 to further phosphorylate H2A.X, thus amplifying \u03b3H2A.X production and promoting homologous recombination repair. Notably, we observe a significant upregulation of STK39 in pancreatic adenocarcinoma (PAAD) tissues, correlating with heightened resistance to PARPi therapy. Furthermore, we demonstrate the synergistic efficacy of combining STK39 inhibition with PARP inhibitors in suppressing and reversing PAAD growth. This study not only provides new insights into the molecular dynamics of H2A.X phosphorylation but also highlights the therapeutic potential of targeting STK39 to enhance PARPi sensitivity in PAAD (created with BioRender).<\/jats:p>","DOI":"10.1093\/nar\/gkae1099","type":"journal-article","created":{"date-parts":[[2024,11,26]],"date-time":"2024-11-26T11:11:46Z","timestamp":1732619506000},"page":"13881-13895","source":"Crossref","is-referenced-by-count":10,"title":["STK39-mediated amplification of \u03b3-H2A.X promotes homologous recombination and contributes to PARP inhibitor resistance"],"prefix":"10.1093","volume":"52","author":[{"given":"Yi","family":"Xu","sequence":"first","affiliation":[{"name":"State Key Laboratory of Molecular Oncology and Department of Radiation Oncology, National Cancer Center\/National Clinical Research Center for Cancer\/Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College , Panjiayuan Nanli No17, Chaoyang 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