PARP10

PARP10 (also known as ARTD10) is a mono-ADP-ribosyltransferase that catalyzes mono-ADP-ribosylation of target proteins and functions as a regulator of cellular proliferation, transcriptional responses, and genome maintenance^[1][2]. Mechanistically, PARP10 participates in DNA damage tolerance pathways through interactions with proliferating cell nuclear antigen (PCNA), thereby promoting translesion DNA synthesis and replication-associated stress responses^[3][4]. Recent evidence further demonstrates that PARP10 is recruited to nascent single-stranded DNA gaps, where it facilitates RAD18-dependent PCNA ubiquitination and REV1 recruitment, supporting gap filling and preservation of genomic stability under replication stress conditions^[5]. In disease-relevant models, elevated PARP10 activity has been associated with enhanced cellular proliferation, replication fork stability, and tumor growth, suggesting that PARP10 can support adaptation to oncogenic replication stress^[6]. Compared with canonical PARP family members such as PARP1 and PARP2, which primarily catalyze poly-ADP-ribosylation, PARP10 lacks polymer-forming activity and instead functions predominantly as a mono-ADP-ribosyltransferase through a distinct catalytic mechanism that restricts its enzymatic output to MARylation^[2][7]. This biochemical distinction underlies its specialized roles in replication-associated genome maintenance and DNA damage tolerance pathways^[3][5]. For experimental applications, selective PARP10 inhibitors and chemical probes have been developed and are used to investigate PARP10-dependent signaling, DNA repair regulation, and cancer-associated replication stress mechanisms^[7][8].