The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Moe  -  Moesin

Drosophila melanogaster

Synonyms: CG10701, D17, Dmel\CG10701, Dmoe, EMR1, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Moe

  • The protein also becomes highly enriched in pseudopods, microvilli, axons, denticles, the border cell process, and other membrane projections, potentially by binding to endogenous moesin as well as actin [1].

High impact information on Moe


Biological context of Moe

  • This communication demonstrates that mutations in the Drosophila moesin (Dmoe) gene that encodes another actin binding protein result in delocalization of osk mRNA and protein from the posterior subcortical region and, as a consequence, in failure of embryonic germ cell development [6].
  • Independent roles of Drosophila Moesin in imaginal disc morphogenesis and hedgehog signalling [7].
  • In Drosophila, loss of moesin (moe) activity causes incorrect localisation of maternal determinants during oogenesis, failures in rhabdomere differentiation in the eye and alterations of epithelial integrity in the wing imaginal disc [7].
  • DRok regulates at least one of these targets, the membrane cytoskeletal cross-linker DMoesin, via a direct phosphorylation that is required to promote localization of DMoesin to the oocyte cortex [8].
  • The protein 4.1, ezrin, radixin, moesin (FERM) domain of Drosophila Coracle, a cytoplasmic component of the septate junction, provides functions essential for embryonic development and imaginal cell proliferation [9].

Anatomical context of Moe

  • In Dmoe mutant oocytes, the subcortical actin network is detached from the cell membrane, while the polarized microtubule cytoskeleton is unaffected [6].
  • In line with the earlier observations, colocalization of ectopic actin and OSK protein in Dmoe mutants suggests that the actin cytoskeleton anchors OSK protein to the subcortical cytoplasmic area of the Drosophila oocyte [6].
  • ERM (ezrin, radixin, moesin) proteins have been proposed to link transmembrane proteins to the actin cytoskeleton in the apical domain, suggesting a structural role in epithelial cells, and they have been implicated in signalling pathways [2].
  • While Dmoesin is observed in continuous association with the plasma membrane, as is typical for an ERM family protein, Dmerlin is found in punctuate structures at the membrane and in the cytoplasm [10].
  • Our results show an essential structural role for Moesin in photoreceptor morphology [11].

Associations of Moe with chemical compounds

  • As a result of these studies, we propose that the merlin protein has unique functions in the cell which differ from those of other ERM family members [10].
  • In vitro assays show that NIK interacts directly with ERM proteins, binding their N termini and phosphorylating a conserved C-terminal threonine [12].
  • Both this PDZ1-2 site and the I3 domain associate with a 30-kD NH2-terminal domain of protein 4.1 that is conserved in ezrin/radixin/moesin (ERM) proteins [13].

Other interactions of Moe

  • Thus, Moesin functions in maintaining epithelial integrity by regulating cell-signalling events that affect actin organization and polarity [2].


  1. GFP-moesin illuminates actin cytoskeleton dynamics in living tissue and demonstrates cell shape changes during morphogenesis in Drosophila. Edwards, K.A., Demsky, M., Montague, R.A., Weymouth, N., Kiehart, D.P. Dev. Biol. (1997) [Pubmed]
  2. Moesin functions antagonistically to the Rho pathway to maintain epithelial integrity. Speck, O., Hughes, S.C., Noren, N.K., Kulikauskas, R.M., Fehon, R.G. Nature (2003) [Pubmed]
  3. Dmoesin controls actin-based cell shape and polarity during Drosophila melanogaster oogenesis. Polesello, C., Delon, I., Valenti, P., Ferrer, P., Payre, F. Nat. Cell Biol. (2002) [Pubmed]
  4. Phosphorylation and activity of the tumor suppressor Merlin and the ERM protein Moesin are coordinately regulated by the Slik kinase. Hughes, S.C., Fehon, R.G. J. Cell Biol. (2006) [Pubmed]
  5. Crumbs interacts with moesin and beta(Heavy)-spectrin in the apical membrane skeleton of Drosophila. Médina, E., Williams, J., Klipfell, E., Zarnescu, D., Thomas, G., Le Bivic, A. J. Cell Biol. (2002) [Pubmed]
  6. MOESIN crosslinks actin and cell membrane in Drosophila oocytes and is required for OSKAR anchoring. Jankovics, F., Sinka, R., Lukácsovich, T., Erdélyi, M. Curr. Biol. (2002) [Pubmed]
  7. Independent roles of Drosophila Moesin in imaginal disc morphogenesis and hedgehog signalling. Molnar, C., de Celis, J.F. Mech. Dev. (2006) [Pubmed]
  8. Drosophila Rho-kinase (DRok) is required for tissue morphogenesis in diverse compartments of the egg chamber during oogenesis. Verdier, V., Johndrow, J.E., Betson, M., Chen, G.C., Hughes, D.A., Parkhurst, S.M., Settleman, J. Dev. Biol. (2006) [Pubmed]
  9. The protein 4.1, ezrin, radixin, moesin (FERM) domain of Drosophila Coracle, a cytoplasmic component of the septate junction, provides functions essential for embryonic development and imaginal cell proliferation. Ward, R.E., Schweizer, L., Lamb, R.S., Fehon, R.G. Genetics (2001) [Pubmed]
  10. Distinct cellular and subcellular patterns of expression imply distinct functions for the Drosophila homologues of moesin and the neurofibromatosis 2 tumor suppressor, merlin. McCartney, B.M., Fehon, R.G. J. Cell Biol. (1996) [Pubmed]
  11. Moesin contributes an essential structural role in Drosophila photoreceptor morphogenesis. Karagiosis, S.A., Ready, D.F. Development (2004) [Pubmed]
  12. The Nck-interacting kinase phosphorylates ERM proteins for formation of lamellipodium by growth factors. Baumgartner, M., Sillman, A.L., Blackwood, E.M., Srivastava, J., Madson, N., Schilling, J.W., Wright, J.H., Barber, D.L. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  13. Two independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domain. Lue, R.A., Brandin, E., Chan, E.P., Branton, D. J. Cell Biol. (1996) [Pubmed]
WikiGenes - Universities