Ubiquitin-specific peptidase 13 (USP13)

Ubiquitin-specific peptidase 13 is a member of the ubiquitin-specific protease (USP) family, playing a pivotal role in the deubiquitination process—a form of post-translational modification that influences protein stability, function, and location. USP13 possesses a zinc finger (ZnF) domain, a catalytic USP domain, and two ubiquitin-associated (UBA) domains, allowing it to recognize and remove K48- and K63-linked polyubiquitin chains from key substrates such as PTEN, cyclin D1, Beclin-1, and others. Through this activity, USP13 regulates diverse processes: it stabilizes proteins (preventing degradation), controls cell cycle progression, facilitates DNA damage response, supports energy metabolism, and modulates autophagy. Its dysregulation contributes to various pathological states including cancer, fibrosis, and neurodegenerative diseases, making it a significant target for therapeutic intervention.

Other names

Ubiquitin-specific protease 13USP13

Inhibition of USP13 increases ubiquitination and proteasomal degradation of its substrates (e.g., cyclin D1, PTEN, Beclin-1). Inhibition can block cell proliferation, induce cell cycle arrest, or alter autophagic flux, depending on substrate and tissue context.