Ubiquitin specific peptidase 10 (USP10)

Ubiquitin specific peptidase 10 (USP10) is a member of the ubiquitin-specific protease (USP) family of deubiquitinating enzymes. It specifically cleaves ubiquitin from conjugated protein substrates and is involved in diverse cellular processes including protein degradation, DNA damage response, autophagy, cell signaling, and immune regulation. USP10 acts through its cysteine protease activity and regulates several clinically significant targets such as p53, Beclin1, CFTR, and PTEN. It localizes in both the nucleus and cytoplasm and modulates cell fate in a context-dependent manner, functioning as either a tumor suppressor or oncogene depending on cellular background and pathological state. USP10 is being investigated as a therapeutic target for cancer, neurodegenerative diseases, and conditions involving disrupted ubiquitin signaling[1][3][4][5][9][11].

Other names

Ubiquitin carboxyl-terminal hydrolase 10KIAA0190UBPODeubiquitinating enzyme 10Ubiquitin thioesterase 10Ubiquitin-specific-processing protease 10ubiquitin specific protease 10ubiquitin thiolesterase 10

USP10 inhibitors block deubiquitinating activity leading to increased ubiquitination and degradation of USP10 substrates (such as p53, Beclin1, CFTR), impacting cell cycle, apoptosis, autophagy, or stress responses[1][9].