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The Drosophila rhodopsin cytoplasmic tail domain is required for maintenance of rhabdomere structure

Syed Tariq Ahmad^*,1, Michael Natochin, Nikolai O. Artemyev and Joseph E. O’Tousa^*,2

^* Department of Biological Sciences, University of Notre Dame, Notre Dame, Indiana, USA; and

Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa, USA

² Correspondence: Department of Biological Sciences, University of Notre Dame, Notre Dame, IN 46556, USA. E-mail: jotousa{at}nd.edu

The ninaE-encoded Rh1 rhodopsin is the major light-sensitive pigment expressed in Drosophila R1–6 photoreceptor cells. Rh1 rhodopsin localizes to and is essential for the development and maintenance of the rhabdomere, the specialized membrane-rich organelle that serves as the site of phototransduction. We showed previously that the vertebrate bovine rhodopsin (Rho) is expressed and properly localized in Drosophila photoreceptor cells. Drosophila photoreceptors expressing only Rho have normal rhabdomere structure at young ages, but the rhabdomeres are not maintained and show extensive disorganization by 7–10 days of age. A series of Rho-Rh1 opsin chimeric rhodopsins were used to identify Rh1 domains required for maintenance of rhabdomeric structure. The results show that the Rh1 rhodopsin cytoplasmic tail domain, positioned to interact with cytoplasmic structural components, plays a major role in promoting rhabdomeric organization.—Ahmad, S. T., Natochin, M., Artemyev, N. O., O’Tousa J. E. The Drosophila rhodopsin cytoplasmic tail domain is required for maintenance of rhabdomere structure.

Key Words: bovine rhodopsin • microvillus • retinal degeneration