Mono-ADP-ribosylation by PARP10 and PARP14 in genome stability.
Level 5 - mechanism / opinion, no new human data
Narrative review of cellular mechanisms and preclinical pharmacology with no primary clinical data.
PubMed 36814782 · doi:10.1093/narcan/zcad009
What was done
The authors reviewed the literature regarding mono-ADP-ribosylation (MARylation) catalyzed by ADP-ribosyltransferases, focusing on the biological functions of PARP10 and PARP14. The review synthesizes evidence on their roles in DNA damage repair, genome stability, carcinogenesis, response to chemotherapy, and early-stage small-molecule inhibitors targeting these enzymes.
What was found
The abstract provides a qualitative summary rather than numerical data. It notes that while PARP1 and PARP2 (poly-ADP-ribosylation catalysts) are well characterized, the mono-ADP-ribosyltransferases PARP10 and PARP14 are emerging as key regulators of genomic maintenance, cancer progression, and therapeutic sensitivity.
Why it matters
Targeting poly-ADP-ribose polymerases (PARP1/2) is an established oncology strategy, and elucidating the distinct mono-ADP-ribosylating functions of PARP10 and PARP14 may uncover novel therapeutic targets and mechanisms of chemoresistance.
Limits
This is a narrative review without systematic search methodology, meta-analysis, or new primary empirical data. The abstract reports no quantitative effect sizes, clinical efficacy data, or specific pharmacodynamic parameters for PARP10/14 inhibitors.
Cited by
- supports The PARP enzyme superfamily contains approximately 16 to 17 members, many of which modify proteins with single ADP-ribose units rather than synthesizing ADP-ribose polymers.