USP15

USP15, also known as Ubiquitin-specific protease 15, is a deubiquitinating enzyme (DUB) encoded by the USP15 gene in humans. It belongs to the ubiquitin-specific protease family, which are enzymes that cleave ubiquitin from protein substrates. Ubiquitination is a post-translational modification that plays a critical role in various cellular processes, including protein degradation, signal transduction, and DNA repair. USP15 specifically removes polyubiquitin chains from its target proteins.

The precise substrates and functions of USP15 are still areas of active research. However, studies have indicated its involvement in several cellular pathways. It has been implicated in regulating the DNA damage response, where it can deubiquitinate proteins involved in sensing and repairing DNA breaks. Furthermore, USP15 has been linked to the regulation of TGF-beta signaling, a crucial pathway for cell growth, differentiation, and development. Dysregulation of USP15 activity has been observed in certain diseases, including cancer, suggesting its potential role as a therapeutic target. Research continues to elucidate the full spectrum of USP15's cellular roles and its implications in health and disease.