Moesin (MSN)

Moesin is a member of the Ezrin-Radixin-Moesin (ERM) family of cytoskeletal adaptor proteins that link the actin cytoskeleton to the plasma membrane, enabling cells to maintain structural integrity and regulate cortical rigidity[1][6][10]. Moesin contains an N-terminal FERM domain that binds membrane proteins and lipids, and a C-terminal domain that interacts with F-actin, with conformational activation regulated by phosphorylation[1][3]. Localized to cellular protrusions such as filopodia, Moesin is critical in shaping cell morphology, promoting apical-basal polarity especially in epithelial cells, and facilitating processes like cell movement, cell-cell recognition, and signal transduction[1][3][7][9]. In neuronal and epithelial contexts, Moesin is essential for morphogenesis, membrane domain organization, and acts antagonistically to Rho signaling to maintain tissue integrity[1][3][5][8]. Dysregulation or altered expression of Moesin and related ERM proteins is implicated in tumorigenesis and cancer cell migration[7]. Moesin is not a classic therapeutic target (not a receptor, enzyme, transporter, etc.), but is highly relevant in cell biology and disease pathology as a key structural and signaling organizer.

Other names

Membrane-organizing extension spike proteinMSN