Ubiquitin specific peptidase 2 (USP2)

Ubiquitin specific peptidase 2 (USP2) is a cysteine protease of the deubiquitinating enzyme family involved in removing ubiquitin moieties from polyubiquitinated protein substrates. It regulates multiple biological pathways, including cell cycle progression by stabilizing cyclins (such as cyclin D1 and cyclin A1), modulation of p53 tumor suppressor signaling via deubiquitination of MDM2 and MDM4, metabolic processes through interaction with PPAR-γ in muscle and regulation of cholesterol uptake in liver, circadian rhythm by affecting core clock proteins, and immune signaling by regulating cytokine responses. Dysregulation of USP2 has been implicated in various diseases, most notably several cancer types, where it promotes tumor cell proliferation and survival, as well as metabolic disorders such as diabetes-related muscle atrophy. USP2 is under investigation as a potential therapeutic target, especially in oncology and metabolic syndrome contexts, but clinical drugs for its direct inhibition are not yet approved.

Other names

Ubiquitin carboxyl-terminal hydrolase 2Deubiquitinating enzyme 2UBP4141 kDa ubiquitin-specific proteaseUbiquitin thioesterase 2Ubiquitin-specific-processing protease 2

Inhibition of the USP2 enzyme to destabilize specific oncogenic proteins (such as cyclin D1, MDM2, MDM4), leading to cell cycle arrest or apoptosis in cancer cells