Ubiquitin specific peptidase 35 (USP35)

Ubiquitin specific peptidase 35 (USP35) is a deubiquitinating enzyme responsible for removing ubiquitin from target proteins, thereby regulating their stability and function. USP35 is a member of the peptidase C19 family, featuring a unique homodimeric structure that is essential for full catalytic activity. It plays crucial roles in cell cycle control—especially mitosis—by stabilizing the chromosomal passenger complex protein Aurora B, regulates mitophagy by delaying PARK2-mediated mitochondrial degradation, and modulates key signaling pathways including NF-κB and type I interferon production. USP35 also interacts with important proteins such as NRF2 and TNIP2, impacting outcomes in cancer, inflammation, and neurodegeneration. Though its direct targeting by drugs remains under investigation, its function and expression are of considerable interest in oncology and immunology. Reduced USP35 expression is frequently observed in tumors, and its loss sensitizes cells to chemotherapy, positioning it as a potential biomarker and therapeutic target.

Other names

Ubiquitin carboxyl-terminal hydrolase 35KIAA1372USP34Deubiquitinating enzyme 35Ubiquitin thioesterase 35Ubiquitin-specific-processing protease 35

Catalytic removal of ubiquitin moieties from substrate proteins, thereby preventing their proteasomal degradation and modulating activity/stability. For hypothetical inhibitors: likely inhibition of deubiquitinating activity, leading to increased degradation of proteins such as Aurora B and NRF2, impairing cell cycle progression and survival.