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Ring finger protein 170 is an E3 ubiquitin ligase embedded in the endoplasmic reticulum membrane, defined by its RING domain. It mediates ubiquitination and regulated degradation of inositol 1,4,5-trisphosphate receptors (IP3Rs), crucial for calcium signaling, through the ER-associated degradation pathway. RNF170 is recruited to IP3Rs by the ERLIN1/ERLIN2 membrane protein complex. It also inhibits TLR3-triggered innate immune responses by catalyzing K48-linked polyubiquitination and proteasomal degradation of TLR3, an important pattern-recognition receptor in antiviral immunity. Genetic mutations in RNF170 cause spastic paraplegia 85 and autosomal dominant sensory ataxia. As a RING finger E3 ligase, RNF170 exemplifies a critical node in protein homeostasis, signaling, and disease susceptibility.
Drugs targeting RNF170 would theoretically modulate its ubiquitin ligase activity, either inhibiting or enhancing ubiquitination of proteins such as the IP3 receptor or TLR3, thereby affecting protein turnover and signaling cascades
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