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First published online 14 January 2004
doi: 10.1242/dev.00976

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Moesin contributes an essential structural role in Drosophila photoreceptor morphogenesis

Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA

^* Author for correspondence (e-mail: dready{at}bilbo.bio.purdue.edu)

Accepted 11 November 2003

Ezrin-Radixin-Moesin (ERM) family proteins organize heterogeneous sub-plasma membrane protein scaffolds that shape membranes and their physiology. In Drosophila oocytes and imaginal discs, epithelial organization, fundamental to development and physiology, is devastated by the loss of Moesin. Here, we show that Moesin is crucial for Drosophila photoreceptor morphogenesis. Beyond its requirement for retinal epithelium integrity, Moesin is essential for the proper assembly of the apical membrane skeleton that builds the photosensitive membrane, the rhabdomere. Moesin localizes to the rhabdomere base, a dynamic locus of cytoskeletal reorganization and membrane traffic. Downregulation of Moesin through RNAi or genetic loss of function profoundly disrupts the membrane cytoskeleton and apical membrane organization. We find normal levels and distribution of Moesin in photoreceptors of a Moesin mutant previously regarded as protein null, suggesting alternative interpretations for studies using this allele. Our results show an essential structural role for Moesin in photoreceptor morphology.

Key words: Moesin, ERM, Morphogenesis, Photoreceptor, Cytoskeleton, F-actin, Drosophila melanogaster

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