DZIP3 is a viral RNA co-sensor for RIG-I that promotes type-I interferon responses

ABSTRACT: RNA-binding E3 ubiquitin ligases have the ability to link RNA regulation to the protein ubiquitination machinery, thereby influencing diverse biological processes. Here, we identify the RNA-binding E3 ubiquitin ligase DZIP3 as an innate immune co-sensor that couples viral RNA recognition to downstream immune signaling. Upon viral infection, binding of viral RNA to the DZIP3 RNA-binding motif induces conformational changes that promote K63-linked auto-ubiquitination, oligomerization, and stabilization of DZIP3. Activated DZIP3 associates with RIG-I and MAVS at the mitochondrial membrane, promoting K63-linked ubiquitination of RIG-I and robust activation of the type-I interferon response. Consequently, DZIP3 depletion impairs host antiviral defense, whereas DZIP3 restricts infection by a bro

SUBMITTER: Rinku Sahu 

PROVIDER: S-SCDT-10_1038-S44318-026-00943-5 | biostudies-other |

REPOSITORIES: biostudies-other