E3 ubiquitin-protein ligase RNF185 (RNF185)

E3 ubiquitin-protein ligase RNF185 is a membrane-associated RING finger protein localizing to the endoplasmic reticulum and mitochondrial outer membranes. It functions as part of protein quality control systems, tagging misfolded and unassembled proteins for degradation in the ERAD pathway, and mediating selective mitochondrial autophagy by catalyzing Lys63-linked polyubiquitination of mitochondrial substrates like BNIP1. RNF185 is upregulated under conditions of ER stress and may protect cells from apoptosis. It has a functional overlap with similar ligases (such as RNF5) in controlling CFTR turnover and is implicated in cellular adaptation to stress, mitochondrial turnover, and possibly regulation of cell survival and innate immune signaling[1][2][4][3][5]. Its direct modulation as a therapeutic target is currently investigational, with implications for protein-folding diseases, autophagy-related pathologies, and cell stress responses.

Other names

Ring finger protein 185RNF185FLJ38628Hypothetical protein FLJ38628BSK65-MONO1, BSK65-MONO2, BSK65-PANC1, BSK65-PANC2, BSK65-TEST1, BSK65-TEST2, BSK65-TEST3RING-type E3 ubiquitin transferase RNF185

No approved drugs with defined mechanisms that target RNF185. Hypothetical mechanisms for experimental modulation include: Inhibition or enhancement of E3 ubiquitin ligase activity; Modulation of ERAD or mitochondrial autophagy pathways; Regulation of CFTR turnover (with theoretical relevance in cystic fibrosis therapy).