USP10

USP10, a deubiquitinating enzyme (DUB), is found in the cytoplasm where it regulates protein stability and function by removing ubiquitin marks. This enzyme's precise cleavage of ubiquitin chains is essential for managing protein degradation and signal transduction pathways. It plays a role in cellular mechanisms including cell division, cycle progression, programmed cell death, and autophagy. It affects the deubiquitination status of key proteins like p53, PCNA, MSH2, Notch, and PTEN. USP10 is particularly noteworthy in cancer biology, as it can modulate tumor development by stabilizing proteins such as p53, which influences DNA damage responses, and by prolonging the half-life of PTEN. The enzyme's influence in cancer is nuanced; it shows potential tumor-suppressing activity in cancers of the cervix and stomach, and its implications in breast cancer are under investigation for possible anti-cancer properties.