USP17L7 Activators

USP17L7, or Ubiquitin Specific Peptidase 17 Like Family Member 7, is part of the USP17 subfamily within the larger group of cysteine protease deubiquitinating enzymes (DUBs). This family of enzymes is recognized for its role in removing ubiquitin from ubiquitinated proteins, thereby altering the fate and function of these substrates. The ubiquitination process is a critical post-translational modification that typically targets proteins for degradation via the proteasome, and DUBs like USP17L7 reverse this process, impacting protein stability and function.Located on chromosome 4q13, the gene encoding USP17L7 is part of a cluster of homologous genes that have been proposed to arise due to gene duplication events. These genes code for enzymes that share a conserved USP catalytic domain, although they may exhibit differences in their expression patterns, substrate specificities, and biological roles.

USP17L7's specific function and the pathways it influences are not as thoroughly characterized as those of some other DUBs. However, the modulation of ubiquitination by USP17L7 is likely to be involved in various cellular mechanisms, including signal transduction, regulation of the cell cycle, and apoptosis. DUBs, including USP17L7, play essential roles in maintaining cellular homeostasis and can be involved in the pathogenesis of numerous diseases, such as cancer and neurodegenerative disorders.The expression of USP17L7 can be induced by certain stimuli, such as cytokines, which points to a possible involvement in immune and inflammatory responses. Through its deubiquitinating activity, USP17L7 contributes to the dynamic regulation of protein function within the cell, influencing crucial cellular decisions, such as those related to cell growth, survival, and adaptation to environmental stress.