E3 ubiquitin-protein ligase RNF135 (RNF135)

E3 ubiquitin-protein ligase RNF135 (RNF135) is an enzyme characterized by an N-terminal RING finger domain and C-terminal SPRY and PRY motifs, functioning primarily as an E3 ubiquitin ligase[1][2][3]. It acts to ubiquitinate RIG-I (retinoic acid-inducible gene I), thereby promoting RIG-I-mediated activation of the antiviral innate immune response, notably type I interferon production[2][4][6]. RNF135 is implicated in the regulation of gene transcription, protein degradation, cell proliferation, cell cycle progression, migration, and autophagy, with a critical role in antiviral immunity and tumor progression[1][3][5]. Dysregulation or altered expression of RNF135 has been observed in various cancers, including glioblastoma and lung adenocarcinoma, and is associated with prognosis and possibly with oncogenic transformation[1][3][5]. RNF135 also acts as a biomarker and potential therapeutic target in certain malignancies, and genetic alterations can contribute to overgrowth syndromes and modify risk in neurofibromatosis type 1[1][3]. There are currently no clinically approved drugs known to directly target RNF135, nor are there well-defined drug mechanisms or safety profiles for RNF135 inhibitors; concerns for potential therapeutic targeting include impacts on host antiviral defenses and cellular proliferation control.

Other names

RipletRING finger protein 135REULL13MGC13061RIG-I E3 ubiquitin ligaseRING finger protein leading to RIG-I activationRING-type E3 ubiquitin transferase RNF135MMFD