UV excision repair protein RAD23 homolog B (RAD23B)

UV excision repair protein RAD23 homolog B (RAD23B) is a human protein central to DNA repair, primarily through participation in nucleotide excision repair (NER) and recognition of DNA lesions in complex with XPC[1][3][5][6]. RAD23B serves as an adaptor for the proteasome, binding polyubiquitinated substrates via its ubiquitin-like (UBL) and ubiquitin-associated (UBA) domains and mediating protein turnover, protein quality control, and cell cycle regulation[2][5][6]. It is implicated in cancer development through its roles in DNA repair capacity, susceptibility to promoter methylation, and involvement in chemoresistance[1][3][4][5]. RAD23B interacts with proteins such as PSMD4, Ataxin 3, and p53, and deficiency or silencing of RAD23B heightens cancer risk due to impaired DNA repair. While not a direct therapeutic drug target, its levels and function can influence cancer prognosis and response to therapy, particularly DNA-damaging agents[1][3][4][5].

Other names

HR23BhHR23Bp58HHR23BP58XP-C repair-complementing complex 58 kDa proteinXP-C repair complementing proteinRAD23 homolog Bnucleotide excision repair proteinRAD23, yeast homolog of BRAD23B[1][5][7]

Drugs targeting the NER pathway or acting as DNA-damaging agents (e.g., cisplatin) rely on the NER machinery, including RAD23B, for repair of induced lesions - HDAC inhibitors may affect RAD23B-related pathways by altering gene expression and DNA repair capacity[3][5]