Fbxo7, an F-box protein, is a substrate-recognition component of the SCF complex. It functions as an E3 ubiquitin ligase, recognizing and mediating ubiquitination of substrates, and is also involved in regulating the proteasome complex, mitophagy, cell cycle, cell proliferation, and germ cell differentiation [3]. Mutations in FBXO7 have been associated with Parkinson's disease-15 (PARKIN15), highlighting its importance in neurodegenerative disease research [3,4,5,6,8].

In hepatocellular carcinoma, FBXO7 inhibits serine synthesis by ubiquitinating and degrading PRMT1, which in turn impairs PHGDH methylation and activation, leading to reduced serine synthesis, increased ROS, and inhibited cell growth. Its down-regulation in human HCC tissues is inversely related to PRMT1 and PHGDH methylation levels [1].

In glioblastoma, FBXO7 confers mesenchymal properties and chemoresistance by controlling Rbfox2-mediated alternative splicing. It ubiquitinates Rbfox2, leading to its stabilization and regulating the splicing of mesenchymal genes [2].

In endometrial carcinoma, FBXO7 acts as a tumor suppressor by inhibiting INF2-associated mitochondrial division through ubiquitination and degradation of INF2 [7].

In conclusion, Fbxo7 plays crucial roles in multiple biological processes and diseases. In cancer, it can act as a regulator of tumor-related metabolic pathways, cell phenotypes, and mitochondrial function. In Parkinson's disease, its mutations are associated with the pathogenesis. Functional studies, especially those using genetic models, have been essential in uncovering these roles, providing potential targets for cancer therapy and understanding the pathophysiology of Parkinson's disease.