PARP10 is a mono-ADP-ribosyltransferase that catalyzes the transfer of single ADP-ribose units to target proteins, particularly on glutamate and aspartate residues 1. The enzyme plays critical roles in DNA repair and replication stress response by promoting translesion synthesis through interactions with PCNA and recruitment of RAD18, which leads to PCNA ubiquitination and REV1 polymerase recruitment for nascent strand gap filling 2. PARP10 is essential for stress granule assembly, where it ADP-ribosylates G3BP1 and regulates initial assembly kinetics 3. The protein also modulates mitochondrial function, with its depletion increasing oxidative capacity, reducing superoxide production, and activating AMPK signaling 4. Additionally, PARP10 can ADP-ribosylate RNA at phosphorylated ends, representing a novel form of reversible RNA modification 1. PARP10 is overexpressed in multiple cancer types, particularly breast and ovarian cancers, where it promotes tumorigenesis and correlates with poor prognosis 56. Cancer cells overexpressing PARP10 show dependencies on DNA repair genes like ATM, while PARP10-deficient cells rely on CDK2-Cyclin E1 for survival 5. These findings establish PARP10 as a potential therapeutic target, with selective inhibitors showing promise for cancer treatment 7.