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TC-NER is triggered by the stalling of RNA polymerase II at DNA lesions, leading to the recruitment of TC-NER-specific factors such as the CSA\u2013DDB1\u2013CUL4A\u2013RBX1 cullin\u2013RING ubiquitin ligase complex (CRL<jats:sup>CSA<\/jats:sup>). Despite its vital role in TC-NER, little is known about the regulation of the CRL<jats:sup>CSA<\/jats:sup> complex during TC-NER. Using conventional and cross-linking immunoprecipitations coupled to mass spectrometry, we uncover a stable interaction between CSA and the TRiC chaperonin. TRiC\u2019s binding to CSA ensures its stability and DDB1-dependent assembly into the CRL<jats:sup>CSA<\/jats:sup> complex. Consequently, loss of TRiC leads to mislocalization and depletion of CSA, as well as impaired transcription recovery following UV damage, suggesting defects in TC-NER. Furthermore, Cockayne syndrome (CS)-causing mutations in CSA lead to increased TRiC binding and a failure to compose the CRL<jats:sup>CSA<\/jats:sup> complex. 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