Flapwing Dephosphorylates Merlin and Moesin and Regulates Epithelial Integrity in Drosophila
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Abstract
Merlin is a tumor suppressor protein whose inactivation is associated with familial Neurofibromatosis Type II (NF2) and other sporadic tumors. The growth-suppressive function of Merlin is modulated by reversible phosphorylation. Our previous finding showed the Sterile20 kinase Slik coordinately regulates the activity of Merlin and Moesin in Drosophila melanogaster. Here I report that the Drosophila protein phosphatase 1β flapwing (flw) is involved in the coordinate dephosphorylation of Merlin and Moesin. Flw forms a complex with Merlin and Moesin. Changes in flw expression level lead to corresponding changes in the phosphorylation pattern of Merlin and Moesin. Moreover, reducing flw expression in epithelial cells results in increased membrane-association of Merlin and Moesin and disruption of epithelial integrity. Taken together, flw plays a role in epithelial organization by regulating dephosphorylation of Merlin and Moesin.