Poly(ADP-ribose) polymerase 15 (PARP15)

Poly(ADP-ribose) polymerase 15 (PARP15), also known as ARTD7 or BAL3, is a mono-ADP-ribosyltransferase that belongs to the PARP family of enzymes. Unlike the more well-known PARP1, PARP15 catalyzes the transfer of a single ADP-ribose unit onto target proteins rather than forming long polymers. It is characterized by the presence of macrodomains that can bind to ADP-ribose, allowing it to act as both a writer and a reader of this post-translational modification. Biologically, PARP15 is localized to the cytoplasm and nucleus, where it plays a significant role in the formation of stress granules and the regulation of RNA-protein interactions. In the context of disease, PARP15 is often overexpressed in certain B-cell lymphomas and has been implicated in promoting cell survival under stress conditions. It also plays a role in the innate immune response, particularly in interferon-mediated antiviral pathways. Therapeutic interest in PARP15 focuses on the development of selective inhibitors to treat malignancies or modulate immune responses, though most current compounds are in the early research or preclinical stages.

Other names

ARTD7BAL3B-aggressive lymphoma 3ADP-ribosyltransferase diphtheria toxin-like 7Mono(ADP-ribosyl)transferase PARP15

Inhibition of the catalytic mono-ADP-ribosyltransferase activity to modulate stress granule dynamics or immune signaling pathways.