Overexpression of Ubiquitin-Specific Protease15 (USP15) Promotes Tumor Growth and Inhibits Apoptosis and Correlated With Poor Disease-Free Survival in Hepatocellular Carcinoma.
Clinicopathological and prognostic significance of ubiquitin-specific peptidase 15 and its relationship with transforming growth factor-beta receptors in patients with pancreatic ductal adenocarcinoma.
modifications of USP15 and USP4 by phosphorylation are important for the regulation of their localization required for cellular function in the spliceosome.
Study reports that USP15 affects cancer cell response to PARP inhibitors by regulating homologous recombination repair. USP15 is recruited to DNA double-strand breaks (DSBs) by MDC1. USP15 deubiquitinates BARD1 BRCT domain and promotes BARD1-HP1gamma interaction resulting in BRCA1/BARD1 retention at DSBs. Cancer-associated USP15 mutations with decreased USP15-BARD1 interaction increases PARP inhibitor sensitivity.
First example of isoform-specific deubiquitylase phospho-regulation and a novel role for USP15 in guarding genome integrity. USP15 is required for TOP2A accumulation and USP15 depletion leads to the formation of anaphase chromosome bridges., Phosphorylation
HPV E6 oncoprotein antagonizes the activation of the cytoplasmic innate immune sensor RIG-I by targeting its upstream regulatory enzymes TRIM25 and USP15. We further show that the RIG-I signaling cascade is important for an antiviral innate immune response to HPV16 infection
Study identified USP15 as having recurrent de novo loss of function mutations and discovered evidence supporting two other known genes with recurrent de novo variants (FOXP1 and KDM5B).
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