Ubiquitin specific peptidase 17 like family member 26 (USP17L26)

Ubiquitin specific peptidase 17 like family member 26 (USP17L26, or USP17) is a cysteine-type deubiquitinase enzyme that catalyzes the removal of conjugated ubiquitin from substrate proteins to regulate a variety of essential cellular processes, including protein degradation, cell cycle progression, apoptosis, and migration[1][3]. It is primarily localized in the nucleolus and participates in protein deubiquitination pathways, particularly regulating ubiquitin-dependent protein catabolism[1]. USP17 family members regulate cell proliferation and survival and modulate the trafficking and stability of key cell surface receptors, such as platelet-derived growth factor receptor beta (PDGFRβ)[3]. Dysregulation of USP17 expression or activity can lead to defects in cell cycle control and cell viability and may play roles in cancer and other proliferative diseases[3]. No drugs are currently known to selectively target USP17L26, and the functional consequences of its inhibition or overexpression require further study.

Other names

Ubiquitin carboxyl-terminal hydrolase 17-like protein 24USP17L24USP17USP17HUSP17IUSP17JUSP17KUSP17LUSP17MDeubiquitinating enzyme 17Ubiquitin thioesterase 17Ubiquitin-specific-processing protease 17USPL1 (not confirmed)DUB3 (used in literature for the family)U17LO

Inhibition of the enzyme would increase ubiquitination and degradation of substrate proteins Activation or overexpression can prolong the half-life of certain receptors or signaling proteins (as shown for PDGFRβ)[3]