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First published online 23 February 2005
doi: 10.1242/dev.01704

Development 132, 1487-1497 (2005)
Published by The Company of Biologists 2005
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Rab11 mediates post-Golgi trafficking of rhodopsin to the photosensitive apical membrane of Drosophila photoreceptors

Akiko K. Satoh1, Joseph E. O'Tousa2, Koichi Ozaki3 and Donald F. Ready1,*

1 Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA
2 Department of Biological Sciences, University of Notre Dame, Notre Dame, IN 46556, USA
3 Graduate School of Frontier Biosciences, Osaka University, Toyonaka, Osaka 560-0043, Japan

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

Accepted 18 January 2005

In developing Drosophila photoreceptors, rhodopsin is trafficked to the rhabdomere, a specialized domain within the apical membrane surface. Rab11, a small GTPase implicated in membrane traffic, immunolocalizes to the trans-Golgi network, cytoplasmic vesicles and tubules, and the base of rhabdomeres. One hour after release from the endoplasmic reticulum, rhodopsin colocalizes with Rab11 in vesicles at the base of the rhabdomere. When Rab11 activity is reduced by three different genetic procedures, rhabdomere morphogenesis is inhibited and rhodopsin-bearing vesicles proliferate within the cytosol. Rab11 activity is also essential for development of MVB endosomal compartments; this is probably a secondary consequence of impaired rhabdomere development. Furthermore, Rab11 is required for transport of TRP, another rhabdomeric protein, and for development of specialized membrane structures within Garland cells. These results establish a role for Rab11 in the post-Golgi transport of rhodopsin and of other proteins to the rhabdomeric membranes of photoreceptors, and in analogous transport processes in other cells.

Key words: Rhodopsin, Rab11, Retina, Drosophila




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