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Ubiquitin specific peptidase 17-like family member 10 (USP17L10) is a protein-coding deubiquitinating enzyme on chromosome 4 involved in the removal of ubiquitin tags from substrate proteins, thereby modulating multiple cellular processes. It regulates protein stability, cell growth and cycle progression, apoptosis, cell motility, and immune responses. USP17L10 is highly expressed in certain cancers and is essential for chemokine-induced cell migration, functioning downstream of chemokine receptors to facilitate cytoskeletal rearrangement via small GTPase localization. It is implicated in diverse pathological processes, from immunodeficiency syndromes to metastatic cancer, suggesting its importance as a therapeutic target in oncology and immunology[1][2][3][5].
Inhibition of deubiquitinase activity, leading to disrupted protein stabilization and dysregulation of cell proliferation, migration, and apoptosis
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