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Mosaic Eyes is a novel component of the Crumbs complex and negatively regulates photoreceptor apical size.

Establishment of apical-basal cell polarity has emerged as an important process during development, and the Crumbs complex is a major component of this process in Drosophila. By comparison, little is known about the role of Crumbs (Crb) proteins in vertebrate development. We show that the FERM protein Mosaic Eyes (Moe) is a novel regulatory component of the Crumbs complex. Moe coimmunoprecipitates with Ome/Crb2a and Nok (Pals1) from adult eye and in vitro interaction experiments suggest these interactions are direct. Morpholino knockdown of ome/crb2a phenocopies the moe mutations. Moe and Crumbs proteins colocalize apically and this apical localization requires reciprocal protein function. By performing genetic mosaic analyses, we show that moe- rod photoreceptors have greatly expanded apical structures, suggesting that Moe is a negative regulator of Crumbs protein function in photoreceptors. We propose that Moe is a crucial regulator of Crumbs protein cell-surface abundance and localization in embryos.

Pubmed ID: 17092952


  • Hsu YC
  • Willoughby JJ
  • Christensen AK
  • Jensen AM


Development (Cambridge, England)

Publication Data

December 22, 2006

Associated Grants

  • Agency: NEI NIH HHS, Id: EY015420
  • Agency: NEI NIH HHS, Id: R01 EY015420-01
  • Agency: NEI NIH HHS, Id: R01 EY015420-02
  • Agency: NEI NIH HHS, Id: R01 EY015420-03
  • Agency: NEI NIH HHS, Id: R01 EY015420-04

Mesh Terms

  • Animals
  • Eye Proteins
  • Guanylate Cyclase
  • Isoenzymes
  • Membrane Proteins
  • Morphogenesis
  • Mutation
  • Nerve Tissue Proteins
  • Phenotype
  • Protein Kinase C
  • Retinal Rod Photoreceptor Cells
  • Zebrafish
  • Zebrafish Proteins