DNA repair protein RAD51 homolog 1 (RAD51) (RAD51)

Human RAD51 recombinase, officially known as DNA repair protein RAD51 homolog 1, is a central enzyme in the homologous recombination (HR) pathway, which is essential for the error-free repair of DNA double-strand breaks and the maintenance of genomic stability [2, 6, 14]. It functions by forming a helical nucleoprotein filament on single-stranded DNA, facilitating the search for homologous DNA sequences and promoting strand invasion and exchange [1, 13, 21]. In many cancers, RAD51 is overexpressed, which contributes to therapeutic resistance by allowing tumor cells to efficiently repair damage induced by chemotherapy and radiation [4, 7, 17]. Consequently, RAD51 has emerged as a significant therapeutic target, with small-molecule inhibitors like CYT-0851 being developed to sensitize cancer cells to DNA-damaging agents and PARP inhibitors [1, 4, 12]. The protein also plays non-canonical roles in protecting and restarting stalled replication forks, further supporting its role in preventing genomic instability [4, 21]. Beyond its role in cancer, mutations in RAD51 are associated with Fanconi anemia and congenital mirror movement syndrome, highlighting its critical importance in human development and health [2, 6, 21]. Therapeutic strategies targeting RAD51 aim to exploit the synthetic lethality concept, particularly in tumors already deficient in other DNA repair components like BRCA1 or BRCA2 [1, 7, 10]. Monitoring RAD51 foci formation has also become a valuable functional biomarker for assessing homologous recombination deficiency (HRD) in clinical settings [15, 16, 18].

Other names

HsRAD51RECARAD51ABRCC5FANCRHHsRad51HsT16930MRMV2RAD51 recombinase

Inhibition of RAD51 nucleoprotein filament formation on single-stranded DNA, thereby blocking homologous recombination and DNA double-strand break repair [1, 3, 5].