POLL (DNA polymerase lambda) is a multifunctional DNA repair enzyme with critical roles in maintaining genomic stability. Functionally, POLL participates in base excision repair (BER), specifically addressing abasic (AP) sites generated by DNA damage 12. Additionally, POLL contributes to double-strand break (DSB) repair through both non-homologous end joining (NHEJ) and homologous recombination (HR) pathways 234. Mechanistically, POLL possesses three distinct enzymatic activities: template-dependent DNA polymerase activity for accurate DNA synthesis, template-independent terminal transferase activity for gap-filling, and 5'-deoxyribose-5-phosphate (dRP) lyase activity essential for processing AP sites 1562. These complementary activities enable POLL to perform complete BER repair cycles and facilitate DSB resolution. Clinical significance relates to POLL's involvement in preventing genomic mutations; deficiencies in DNA repair polymerases are associated with cancer predisposition and neurological disorders. While direct disease association data were not found in provided abstracts, POLL's roles in multiple repair pathways underscore its importance in maintaining chr10 integrity and protecting against mutation-driven pathologies.