Protein mono-ADP-ribosyltransferase PARP14 (PARP14)

Protein mono-ADP-ribosyltransferase PARP14 (PARP14) is an enzyme of the poly(ADP-ribose) polymerase (PARP) family, acting as a mono-ADP-ribosyltransferase (MARylator) that catalyzes the transfer of single ADP-ribose moieties to target proteins[2][1]. PARP14 contains several domains: three macrodomains (capable of binding mono-ADP-ribose), a WWE domain (involved in protein-protein interactions), RNA recognition motifs, and a C-terminal catalytic site[1][2]. Biologically, PARP14 acts as a transcriptional co-regulator for STAT6, especially in the IL-4 signaling pathway, where it modulates gene expression critical for Th2-type immune responses and anti-inflammatory signaling. PARP14 plays roles in DNA repair, cell survival, cell cycling, and apoptosis, particularly contributing to cancer cell resistance and survival[1][2][3][4]. It is also induced by interferons and participates in host defense responses, including antiviral activity. Disease associations most strongly include certain cancers (multiple myeloma, B-cell lymphoma, hepatocellular carcinoma), inflammatory disorders, allergic diseases, atherosclerosis, and viral infections. Experimental and non-selective inhibitors such as 3-aminobenzamide and PJ34 have shown that PARP14 is a promising therapeutic target in oncology and immunology, although selective PARP14 inhibitors are still in development[1][2][4]. Safety concerns center on possible immune and DNA repair impairment.

Other names

BAL2KIAA1268ARTD8PARP-14pART8ADP-ribosyltransferase diphtheria toxin-like 8B-aggressive lymphoma protein 2Collaborator of STAT6CoaST-6

Inhibitors block mono-ADP-ribosyltransferase activity, suppressing IL-4/STAT6 driven gene transcription and inducing apoptosis in cancer cells