Flapwing Dephosphorylates Merlin and Moesin and Regulates Epithelial Integrity in Drosophila

• Author / Creator

  Yang, Yang

• 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.

• Subjects / Keywords

  • Flapwing
  • Moesin
  • Merlin
  • Epithelial integrity
  • Dephosphorylation
  • Drosophila

• Graduation date

  Fall 2013

• Type of Item

  Thesis

• Degree

  Master of Science

• DOI

  https://doi.org/10.7939/R3RH64

• License

  This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.