USP48 Inhibitors

USP48, a member of the ubiquitin-specific protease (USP) family, serves as a vital regulator of cellular processes by modulating the ubiquitination status of target proteins. Within the ubiquitin-proteasome system (UPS), USP48 functions as a deubiquitinase (DUB), counteracting the degradation of specific proteins targeted for ubiquitination. Its role extends to the regulation of various cellular pathways, including DNA repair, protein homeostasis, and signal transduction. Through its deubiquitination activity, USP48 maintains the stability and activity of key signaling molecules, ensuring proper cellular function and response to internal and external stimuli.

Inhibition of USP48 represents a strategic approach to modulating cellular processes and interfering with specific signaling pathways implicated in disease pathogenesis. Various inhibitors targeting USP48 have been developed to disrupt its deubiquitinase activity, leading to proteasomal degradation and down-regulation of USP48 levels. These inhibitors exert their effects by interfering with the catalytic activity of USP48 or by promoting its degradation via the ubiquitin-proteasome system. By inhibiting USP48, these compounds offer a means to manipulate cellular pathways regulated by USP48, impacting cellular proliferation, apoptosis, and DNA repair processes.