Ubiquitin specific peptidase 17 like family member 29 (USP17L29)

Ubiquitin specific peptidase 17 like family member 29 (USP17L29) is a member of the deubiquitinating enzyme family, functioning as a cysteine-type peptidase that removes ubiquitin moieties from specific proteins, thereby regulating multiple cellular processes such as cell proliferation, cell cycle progression, apoptosis, and cell migration. USP17L29 is rapidly induced in response to cytokine and chemokine stimulation and is necessary for both directional and random cell motility, acting downstream of chemokine receptors to facilitate cytoskeletal rearrangement via small GTPases. Its role in cell migration, proliferation, and survival implicates USP17L29 as a potential therapeutic target in inflammation, immune regulation, and cancer, particularly in processes related to metastasis and tissue invasion. No clinically approved drugs specifically target USP17L29, and inhibition may disrupt essential biological functions in both normal and malignant cells.

Other names

Ubiquitin carboxyl-terminal hydrolase 17-like protein 24USP17L24USP17USP17HUSP17IUSP17JUSP17KUSP17LUSP17MDeubiquitinating enzyme 17Ubiquitin thioesterase 17Ubiquitin-specific-processing protease 17

Inhibition of protein deubiquitination (hypothetical for investigational agents targeting DUB activity); Suppression of cell migration and proliferation if deubiquitinase activity is blocked