{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Llerena Schiffmacher DA"],"funding":["European Molecular Biology Organization","Deutsche Forschungsgemeinschaft","Deutsche Forschungsgemeinschaft (German Research Foundation)","NIA NIH HHS","U.S. Department of Health &amp; Human Services | NIH | National Institute on Aging","European Molecular Biology Organization (EMBO)","Dutch Research Council (NWO)","ZonMw","European Joint Project on Rare Diseases RD20-113, acronym TC-NER"],"pagination":["6374"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11286758"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["Transcription-blocking DNA lesions are specifically targeted by transcription-coupled nucleotide excision repair (TC-NER), which removes a broad spectrum of DNA lesions to preserve transcriptional output and thereby cellular homeostasis to counteract aging. TC-NER is initiated by the stalling of RNA polymerase II at DNA lesions, which triggers the assembly of the TC-NER-specific proteins CSA, CSB and UVSSA. CSA, a WD40-repeat containing protein, is the substrate receptor subunit of a cullin-RING ubiquitin ligase complex composed of DDB1, CUL4A/B and RBX1 (CRL4<sup>CSA</sup>). Although ubiquitination of several TC-NER proteins by CRL4<sup>CSA</sup> has been reported, it is still unknown how this complex is regulated. To unravel the dynamic molecular interactions and the regulation of this c"],"journal":["Nature communications"],"pubmed_title":["The small CRL4<sup>CSA</sup> ubiquitin ligase component DDA1 regulates transcription-coupled repair dynamics."],"pmcid":["PMC11286758"],"funding_grant_id":["P01 AG017242","733050810","714.017.003","ALTF 1159-2019","496650118"],"pubmed_authors":["Verlaan-de Vries M","Sixma TK","Bezstarosti K","Lee SH","Hoeijmakers JHJ","Theil AF","van Attikum H","Ogi T","Gonzalo-Hansen C","Vermeulen M","Akita M","Vertegaal ACO","Marteijn JA","Demmers JAA","Kliza KW","Vermeulen W","Lans H","Pines A","Llerena Schiffmacher DA","Helfricht A"],"additional_accession":[]},"is_claimable":false,"name":"The small CRL4<sup>CSA</sup> ubiquitin ligase component DDA1 regulates transcription-coupled repair dynamics.","description":"Transcription-blocking DNA lesions are specifically targeted by transcription-coupled nucleotide excision repair (TC-NER), which removes a broad spectrum of DNA lesions to preserve transcriptional output and thereby cellular homeostasis to counteract aging. TC-NER is initiated by the stalling of RNA polymerase II at DNA lesions, which triggers the assembly of the TC-NER-specific proteins CSA, CSB and UVSSA. CSA, a WD40-repeat containing protein, is the substrate receptor subunit of a cullin-RING ubiquitin ligase complex composed of DDB1, CUL4A/B and RBX1 (CRL4<sup>CSA</sup>). Although ubiquitination of several TC-NER proteins by CRL4<sup>CSA</sup> has been reported, it is still unknown how this complex is regulated. To unravel the dynamic molecular interactions and the regulation of this c","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-03T00:17:12.879Z","creation":"2025-04-04T07:43:21.524Z"},"accession":"S-EPMC11286758","cross_references":{"pubmed":["39075067"],"doi":["10.1038/s41467-024-50584-7"]}}