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Ubiquitin specific peptidase 17 like family member 19 (USP17L19) is a member of the USP17 subfamily of deubiquitinating enzymes (DUBs), responsible for removing ubiquitin from protein substrates. These enzymes regulate protein turnover and stability, and USP17L19 is predicted to influence cell proliferation, cell cycle progression, apoptosis, and cell migration. The USP17 family is rapidly induced by chemokines and cytokines, participating downstream of receptor signaling, notably in GTPase-dependent cell motility and cytoskeletal rearrangement. USP17 family DUBs, including USP17L19, are considered druggable targets in cancer and inflammatory diseases due to their roles in cellular migration and proliferation. However, drug development and characterization of USP17L19-specific pharmacology remain at a preclinical stage.
Inhibition of USP17L19 would block deubiquitination of specific substrates, affecting cell cycle progression, migration, and possibly apoptotic regulation
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