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Pathway-specific repair factors determine its recruitment to specific DNA substrates. Saw1 recruits it to 3\u2032 non-homologous tail recombination intermediates, while Rad14 recruits it to UV-lesions repaired by nucleotide excision repair. However, the exact recruitment mechanisms are unknown. We determined the cryo-EM structure of the Rad1\u2013Rad10\u2013Saw1 complex at 3.7 \u00c5 resolution. The structure reveals that Saw1 wraps around the helicase-like domain of Rad1 defining an extensive interface. Point mutations on this surface disrupt the interaction and inhibit double-strand break repair without compromising nucleotide excision repair, indicating that Rad1\u2013Rad10 uses different surfaces to interact with pathway-specific repair factors. Mutational analyses confirm that Rad14 and Saw1 bind to opposite faces of Rad1. Accordingly, defects on the Rad14-binding interface disrupt nucleotide excision repair without affecting double-strand break repair. In contrast to XPF\u2013ERCC1, Rad1\u2013Rad10 does not adopt an auto-inhibited conformation in the absence of DNA indicating that substrate binding may be regulated differently across species. Collectively, our data provide structural insight into how targeting factors interact with Rad1\u2013Rad10 to recruit it to different DNA repair intermediates.<\/jats:p>","DOI":"10.1093\/nar\/gkag888","type":"journal-article","created":{"date-parts":[[2026,9,5]],"date-time":"2026-09-05T13:51:33Z","timestamp":1788616293000},"source":"Crossref","is-referenced-by-count":0,"title":["Rad1\u2013Rad10 uses different interfaces to interact with pathway-specific DNA repair factors"],"prefix":"10.1093","volume":"54","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1215-7828","authenticated-orcid":false,"given":"Javier","family":"Rodr\u00edguez\u00a0Gonz\u00e1lez","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Centre de Recherche en Biologie Structurale, McGill University , Montreal, QC H3G 0B1 ,","place":["Canada"]},{"name":"Centre de Recherche en Biologie Structurale, McGill University , Montreal, QC H3G 0B1 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