PARP14 is regulated by the PARP9/DTX3L complex and promotes interferon γ-induced ADP-ribosylation

ABSTRACT: Protein ADP-ribosylation plays important but ill-defined roles in antiviral signalling cascades such as the interferon response. Several viruses of clinical interest, including coronaviruses, express hydrolases that reverse ADP-ribosylation catalysed by host enzymes, suggesting an important role for this modification in host-pathogen interactions. However, which ADP-ribosyltransferases mediate host ADP-ribosylation, what proteins and pathways they target, and how these modifications affect viral infection and pathogenesis is currently unclear. Here, we show that host ADP-ribosyltransferase activity induced by IFNγ signalling depends on PARP14 catalytic activity, and that the PARP9/DTX3L complex is required to uphold PARP14 protein levels via post-translational mechanisms. Both the PARP9/DT

SUBMITTER: Victoria, Chaves Ribeiro 

PROVIDER: S-SCDT-10_1038-S44318-024-00125-1 | biostudies-other |

REPOSITORIES: biostudies-other