dsRNA:Ub-RIG-I:TRIM25 dsRNA bound to RIG-I K63-polyubiquitin RIG-I E3 ubiquitin ligases K-63-linked polyubiquitination of RIG-I Authored: Garapati, P V, 2010-08-02 EC Number: 6.3.2.19 Edited: Garapati, P V, 2010-08-02 On viral infection RIG-I undergoes robust ubiquitination at its N-terminal CARD region. TRIM25 a member of tripartite motif (TRIM) protein family and Riplet/RNF135/REUL are the ubiquitin E3 ligases involved in K-63-linked polyubiquitination of RIG-I. TRIM25 contains a cluster of domains including a RING-finger domain, a B box/coiled-coil domain and a SPRY domain. The interaction is mediated by the SPRY domain of TRIM25 and the N-terminal CARDs of RIG-I. The polyubiquitin chains added by TRIM25 are unanchored Lys-172 (K-172) residue of RIG-I is critical for efficient TRIM25-mediated ubiquitination and for IPS-1 binding, as well as the ability of RIG-I to induce antiviral signal transduction. RING-finger protein, RNF135 specifically associate with RIG-I through its PRY and SPRY domains. The Lys 154, 164, and 172 residues of the RIG-I CARD domain were determined to be critical for efficient RNF135-mediated ubiquitination and for the ability of RIG-I to induce antiviral signal transduction. (Michaela et al, Goa et al) Pubmed17392790 Pubmed19017631 Pubmed19484123 Pubmed20403326 Reactome Database ID Release 43918224 Reactome, http://www.reactome.org ReactomeREACT_25220 Reviewed: Kawai, T, Akira, S, 2010-10-30 has a Stoichiometric coefficient of 2