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This nuclease is known to be important for nucleotide excision repair, interstrand crosslink repair, and DNA double-strand repair. We found that the arginine methyltransferase, CARM1\/PRMT4, is essential for XPF stabilization and maintenance of intracellular protein levels. Loss of CARM1 results in a decrease in XPF protein levels and a concomitant decrease in ERCC1 protein. A similar destabilization of XPF protein was observed in cells expressing a mutant in which XPF arginine 568 was replaced by lysine. Loss of CARM1 impaired XPF\u2013ERCC1 accumulation at the site of damage and delayed removal of cyclobutane pyrimidine dimers by UV. As a result, CARM1-deficient cells showed increased UV sensitivity. Our results provide insight into the importance of CARM1 not only in the mechanism of XPF\u2013ERCC1 complex stabilization but also in the maintenance of genome stability.<\/jats:p>","DOI":"10.1093\/nar\/gkaf355","type":"journal-article","created":{"date-parts":[[2025,4,30]],"date-time":"2025-04-30T09:24:50Z","timestamp":1746005090000},"source":"Crossref","is-referenced-by-count":2,"title":["CARM1\/PRMT4 facilitates XPF\u2013ERCC1 heterodimer assembly and maintains nucleotide excision repair activity"],"prefix":"10.1093","volume":"53","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7508-055X","authenticated-orcid":false,"given":"Hiroyuki","family":"Niida","sequence":"first","affiliation":[{"name":"Hamamatsu University School of Medicine Department of Molecular Biology, , 1-20-1 Handayama , Hamamatsu , Shizuoka 431-3192 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