The effects of wild-type Usp24 or catalytically inactive USP24 on EgfrL858R-driven lung tumor specimens.
Ubiquitin-specific peptidase 24 (USP24), a cysteine protease, functions as deubiquitinating enzyme that recognizes and removes ubiquitin from the target protein. USP24 is overexpressed in various cancers and regulates the stability of proteins involved in cancer metastasis, cancer stemness, and drug resistance. While the expression profile alteration in tumor microenvironment upon USP24 inhibition is unrevealed. Through RNA-seq, we have characterized that USP24 catalytically inactivation upregulates activation of immune response and lymphocyte activation-related genes in lung tumors from EgfrL858RUsp24C1695A mice Overall design: Comparative gene expression profiling analysis of RNA-seq for lung tumor specimens from TetO-EgfrL858RUsp24WT or TetO-EgfrL858RUsp24C1695A mice after ten weeks of doxycycline-induction