Ubiquitin-specific protease 7 promotes the growth and oncogenic potential of acute myeloid leukemia cells through the deubiquitination and upregulation of LRRK2.

ABSTRACT: Leucine-rich repeat kinase 2 (LRRK2), a large protein with kinase and GTPase activities, regulates various cellular pathways, including autophagy, endocytosis, and mitochondrial dynamics. LRRK2, extensively studied in the context of Parkinson's disease is functionally impaired in other pathological conditions as well, including inflammatory bowel disease, cancer, and cardiovascular diseases. Despite its critical functions, the mechanisms controlling LRRK2 protein stability are not fully understood. Recent studies suggest that the ubiquitin-proteasome system plays a key role in regulating LRRK2 stability. However, the relationship between deubiquitinating enzymes and LRRK2 has not been fully understood. In this study, we identified ubiquitin-specific protease 7 (USP7) as the novel deubiquit

SUBMITTER: Park JH 

PROVIDER: S-EPMC12510031 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature