The deubiquitinase USP36 funtions through catalytic-dependent and catalytic-independent mechanisms in Drosophila.

ABSTRACT: Deubiquitinases (DUBs) form a specific class of proteases removing ubiquitin from target proteins. They are involved in the regulation of many cellular processes including cell growth and proliferation. Among them, USP36 is a key regulator of the oncogenic transcription factor c-Myc, preventing its degradation by the proteasome. These 2 proteins form an evolutionary conserved complex providing the opportunity to investigate USP36 mechanisms of action in vivo in a genetically tractable model such as Drosophila melanogaster. Null mutants of dUsp36 die early during larval development and exhibit severe growth defects. Strikingly, we report here that flies expressing a catalytically inactive version of dUSP36 produced by CRISPR/Cas9 gene editing survive to adulthood with only minor growth defe

SUBMITTER: Coirry C 

PROVIDER: S-EPMC12406001 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature