Ring finger protein 5 mediates STING degradation through ubiquitinating K135 and K155 in a teleost fish.

ABSTRACT: Stimulator of interferon genes (STING) is a key connector protein in interferon (IFN) signaling, crucial for IFN induction during the activation of antiviral innate immunity. In mammals, ring finger protein 5 (RNF5) functions as an E3 ubiquitin ligase, mediating STING regulation through K150 ubiquitylation to prevent excessive IFN production. However, the mechanisms underlying RNF5's regulation of STING in teleost fish remain unknown. This study investigated the regulatory role of the mandarin fish (Siniperca chuatsi) RNF5 (scRNF5) in the STING-mediated antiviral immune response and identified the specific regulatory sites on scSTING. Furthermore, an examination of scRNF5 expression patterns in virus-infected cells revealed its responsiveness to mandarin fish ra

SUBMITTER: Qin X 

PROVIDER: S-EPMC11668637 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature