Myoferlin (MYOF)

Myoferlin (MYOF) is a large, multi–C2 domain type II transmembrane protein and a member of the ferlin protein family[1][3]. Originally characterized in muscle tissue for its role in membrane fusion and repair, MYOF is now recognized as a multifunctional protein involved in membrane trafficking, endocytosis, and exocytosis across multiple tissues[1][2][3]. In endothelial cells, MYOF regulates the stability and function of important angiogenic receptors—such as VEGFR-2 and Tie-2—by overseeing their recycling, localization, and degradation[2]. MYOF is also present in exosomes and is important for exosome-mediated cellular communication[3]. In cancer, MYOF is frequently overexpressed and associated with tumor growth, metastasis, epithelial to mesenchymal transition, migration, and angiogenesis, making it both a prognostic biomarker and a promising therapeutic target under investigation via small-molecule inhibitors[1][3]. Deficiency or dysfunction of myoferlin is associated with impaired muscle membrane integrity and regeneration, mirroring certain muscular dystrophies[1][2]. In summary, myoferlin is a membrane-associated protein critically involved in cellular fusion, trafficking, and signaling processes with established significance in both health and disease contexts.

Other names

FER1L3Fer-1-like protein 3fer-1-like family member 3KIAA1207HAE7myoferlinFer-1-like 3

Inhibition of C2 domain function (for small molecules such as WJ460)[1] Disruption of membrane fusion and trafficking processes