Fbxo25, an F-box protein, is a component of the SCF protein E3 ubiquitin ligase. It can specifically bind to substrates, regulating multiple biological processes. It is involved in pathways like MAPK signaling and has significance in cell differentiation, proliferation, and cancer-related processes [1,2]. Genetic models, such as gene knockout models, can be valuable for studying its functions.

In cutaneous squamous cell carcinoma (cSCC), stable silencing of Fbxo25 in SCC13 cells led to reduced tumor growth, accompanied by down-regulation of cyclin D1. This suggests Fbxo25 promotes cSCC growth and metastasis through cyclin D1 [1]. In NSCLC, FBXO25 was highly expressed in cancer samples, and its interference could inhibit cell proliferation, invasion, and migration in H1299 cells [4]. In the MAPK signaling pathway, FBXO25 functions as a negative regulator by decreasing MAPK/ERK activity through inhibition of ERK1/2 phosphorylation [2]. In cardiomyocyte development, Fbxo25-mediated SCF ubiquitination pathway regulates the protein levels and activities of Tbx5 and Nkx2-5, and silencing endogenous Fbxo25 suppresses mESC-derived cardiomyocyte differentiation [3].

In conclusion, Fbxo25 plays essential roles in multiple biological processes including cancer development and cardiomyocyte development. Model-based research, especially gene knockout models, has revealed its function in promoting tumor growth in cSCC and NSCLC, and its role in negatively regulating the MAPK signaling pathway and in cardiomyocyte development. This understanding contributes to the study of related diseases and may provide potential therapeutic targets.