RNF11 Protein, Human

RNF11 takes center stage as an essential component of a ubiquitin-editing protein complex, a collaborative ensemble featuring TNFAIP3, ITCH, and TAX1BP1. This complex operates intricately to orchestrate the transient nature of inflammatory signaling pathways, exerting control over TNF- or LPS-mediated activation of NF-kappa-B. RNF11's role extends to promoting the association of TNFAIP3 with RIPK1 post-TNF stimulation. This, in turn, facilitates TNFAIP3's deubiquitination of 'Lys-63' polyubiquitin chains on RIPK1, initiating the formation of 'Lys-48'-polyubiquitin chains that culminate in RIPK1's proteasomal degradation. Furthermore, RNF11 acts as a recruiter, bringing STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, ultimately resulting in SMURF2's degradation by the 26S proteasome. This intricate web of interactions involves 14-3-3 (when phosphorylated), the E3 ubiquitin-ligases NEDD4, ITCH, SMURF2, and WWP1, as well as the E2 ubiquitin-conjugating enzymes UBE2D1 and UBE2N. Noteworthy associations include those with ZNF350, EPS15, STAMBP, TAX1BP1, TNFAIP3, RIPK1, and GGA1, revealing the multifaceted nature of RNF11's regulatory engagements.