Interferon-Induced PARP14-Mediated ADP-Ribosylation in p62 Bodies Requires the Ubiquitin-Proteasome System

ABSTRACT: Biomolecular condensates are cellular compartments without enveloping membranes, enabling them to dynamically adjust their composition in response to environmental changes through post-translational modifications. Recent work has revealed that interferon-induced ADP-ribosylation (ADPr), which can be reversed by a SARS-CoV-2-encoded hydrolase, is enriched within a condensate. However, the identity of the condensate and the responsible host ADP-ribosyltransferase remains elusive. Here, we demonstrate that interferon induces ADPr through transcriptional activation of PARP14, requiring both the physical presence and catalytic activity of PARP14 for condensate formation. Interferon-induced ADPr colocalizes with PARP14 and its associated E3 ligase, DTX3L. These PARP14/ADPr condensates contain ke

SUBMITTER: Rameez Raja 

PROVIDER: S-SCDT-10_1038-S44318-025-00421-4 | biostudies-other |

REPOSITORIES: biostudies-other