USP17L3 Activators

Ubiquitin Specific Peptidase 17 Like Family Member 3 (USP17L3) is a member of the ubiquitin-specific protease (USP) family, which is part of the larger cysteine protease enzyme group. Proteases in this family are known to be deubiquitinating enzymes (DUBs) that cleave ubiquitin moieties from ubiquitin-conjugated protein substrates. The process of deubiquitination is critical for the regulation of protein turnover and signaling, as it rescues proteins from being targeted for degradation by the proteasome, a cellular complex responsible for breaking down unwanted or damaged proteins.

USP17L3, like other members of the USP17 subfamily, is thought to play a role in the regulation of cellular processes such as cell cycle control, apoptosis, and signal transduction. This is achieved by modulating the stability and function of various substrate proteins through the removal of ubiquitin chains. The specificity of USP17L3 for particular substrates and the exact pathways it influences are areas of active research, as is the case with many DUBs.The activity of USP17L3 is tightly regulated within the cell, as uncontrolled deubiquitination can lead to aberrant cell signaling and contribute to disease states, including cancer and neurodegenerative disorders. The expression of USP17L3 may be regulated at both the transcriptional and post-translational levels, ensuring that its deubiquitinating activity is modulated according to cellular needs.