E3 ubiquitin-protein ligase RNF115 (RNF115)

E3 ubiquitin-protein ligase RNF115 (RNF115) is an enzyme that catalyzes the transfer of ubiquitin and SUMO moieties to targeted proteins, regulating diverse cellular processes such as antiviral immunity, cell proliferation, DNA damage repair, vesicle trafficking, and autophagy. RNF115 contains a RING finger domain and functions independently of the classical Cullin-RING ligase (CRL) system. RNF115 is upregulated in breast cancer cells, modulates immune signaling by ubiquitinating key adaptor proteins (notably MAVS and MITA), and is implicated in DNA repair, cell migration, and intracellular compartment fusion. Its expression and function are associated with breast cancer progression and immune disorders, making it a molecular target of interest in oncology and infectious disease research.

Other names

RNF115RING finger protein 115Breast cancer associated gene 2 (BCA2)Rab7-interacting RING finger protein (Rabring 7)Zinc finger protein 364 (ZNF364)RING-type E3 ubiquitin transferase RNF115Zinc finger protein 364RABRING7ZFP364E3 ubiquitin-protein ligase RNF115CL469780

Drugs or experimental reagents that inhibit RNF115 enzymatic activity block its E3 ligase functions, which can affect downstream signaling pathways, cell proliferation, and antiviral immune responses. Inhibition or knockdown of RNF115 sensitizes cancer cells to growth inhibition by agents such as metformin, by affecting AMPK phosphorylation. Theoretical approaches involve blocking its interaction with ubiquitin or substrates such as MAVS/MITA.