USP10 Protein, Human (sf9)

USP10, a hydrolase with versatile substrate specificity, serves as a crucial regulator in multiple cellular processes. Notably, it plays a pivotal role in stabilizing the tumor suppressor p53/TP53 by specifically deubiquitinating it in the cytoplasm under unstressed conditions, counteracting MDM2-mediated degradation. Following DNA damage, USP10 translocates to the nucleus, where it continues to deubiquitinate p53/TP53, contributing to the regulation of the DNA damage response. Additionally, USP10 is integral to a regulatory loop governing autophagy and p53/TP53 levels, mediating the deubiquitination of BECN1. In the context of ribosome biology, USP10 is involved in 40S ribosome subunit recycling, inhibiting stress granule formation and preventing degradation of 40S ribosomal proteins during translation stalling. Beyond its role in protein stability, USP10 participates in endocytic recycling by deubiquitinating CFTR in early endosomes and engages in a TANK-dependent negative feedback response to attenuate NF-kappa-B activation in response to IL1B stimulation or DNA damage. Additionally, USP10 stabilizes TBX21 through deubiquitination, indicating its involvement in diverse cellular pathways.