Protein mono-ADP-ribosyltransferase PARP14 (PARP14) (PARP14)

Protein mono-ADP-ribosyltransferase PARP14 is a multi-domain enzyme belonging to the poly(ADP-ribose) polymerase family, specifically characterized by its mono-ADP-ribosyltransferase activity [1, 11]. Unlike PARP1, which forms long ADP-ribose polymers, PARP14 transfers a single ADP-ribose unit to target proteins, a process known as MARylation [8, 14]. It serves as a critical transcriptional co-regulator, most notably as a collaborator of STAT6 (CoaSt6), where it facilitates IL-4-dependent gene expression and promotes Th2 cell differentiation and B-cell survival [2, 10]. In the context of oncology, PARP14 is frequently overexpressed in malignancies such as multiple myeloma and diffuse large B-cell lymphoma, where it drives pro-survival signaling and metabolic shifts like the Warburg effect [1, 15]. Additionally, it contributes to genomic stability by participating in homologous recombination DNA repair [5, 8]. Due to its dual roles in immune modulation and cancer cell maintenance, PARP14 has emerged as a promising therapeutic target for both allergic inflammatory diseases, such as asthma and atopic dermatitis, and various cancers [1, 13]. Small molecule inhibitors, such as RBN-3143, are currently under investigation to disrupt its catalytic activity and restore normal cellular signaling [12, 13].

Other names

ARTD8BAL2CoaSt6Collaborator of STAT6B-aggressive lymphoma protein 2Poly [ADP-ribose] polymerase 14pART8

Inhibition of mono-ADP-ribosyltransferase activity