USP17L8 Activators

USP17L8, also known as Ubiquitin Specific Peptidase 17 Like Family Member 8, is part of the USP17 (Ubiquitin Specific Peptidase 17) cluster, which comprises a series of closely related deubiquitinating enzymes. These enzymes are characterized by their ability to cleave ubiquitin moieties from ubiquitinated proteins, thereby rescuing them from proteasomal degradation or altering their cellular localization and function.The USP17L8 gene is situated on human chromosome 4q13, within a sequence that contains multiple USP17 family member genes. This group of genes is thought to have expanded through duplication events, resulting in a series of homologs with conserved structural features, particularly within the catalytic domain. Despite this conservation, each member may have distinct expression profiles and biological functions, owing to variations in non-catalytic regions and possibly differential regulation.

The specific activities and substrates of USP17L8 are not entirely clear, but the functional role of DUBs suggests that USP17L8 could be involved in key cellular processes like cell cycle control, DNA repair, signal transduction, and apoptosis. By modulating the ubiquitin status of target proteins, USP17L8 potentially affects their stability, localization, and interactions, which is essential for cellular homeostasis and response to stress.Expression of USP17L8, like other family members, may be inducible by certain stimuli, such as cytokines, growth factors, or cellular stress, indicating a role in the cellular stress response or immune regulation. Given the significant implications of ubiquitination in disease, including cancer, infection, and neurodegeneration, the study of USP17L8 and its interaction with specific substrates is crucial for understanding its contribution to these pathologies.