RNF175 Inhibitors

The landscape of RNF175 inhibitors, surmising RNF175's association with the RING finger E3 ubiquitin ligases, largely comprises compounds that modulate the ubiquitin-proteasome system or affect specific protein-protein interactions. MLN4924 (Pevonedistat), for instance, directly targets and inhibits the NEDD8-activating enzyme. This inhibition has the cascade effect of suppressing the function of E3 ligases, potentially including RNF175.

Compounds like Nutlin-3 and RITA are specific in their action, disrupting the MDM2-p53 interaction. These compounds can modulate RNF175's ubiquitination activity. Meanwhile, molecules like Curcumin, Bortezomib, and Lenalidomide either interfere or inhibit the broader ubiquitin-proteasome system. Such interference impacts the fate of proteins that are targeted for ubiquitination by E3 ligases, like RNF175. Furthermore, Chloroquine's ability to modify lysosomal function might reshape how RNF175 targets proteins for lysosomal degradation. MG132 and Celastrol are proteasome inhibitors, affecting the degradation of proteins ubiquitinated by RNF175. By altering the degradation pathway, the functional landscape of RNF175 can be modulated. Similarly, Bestatin's protease inhibitory action might influence the proteolytic fate of proteins that undergo ubiquitination by RNF175.