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Published online May 21, 2007
doi:10.1083/jcb.200610157
The Journal of Cell Biology, Vol. 177, No. 4, 659-669
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Li et al.
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Article

 Myosin V, Rab11, and dRip11 direct apical secretion and cellular morphogenesis in developing Drosophila photoreceptors

Bingbing X. Li, Akiko K. Satoh, and Donald F. Ready

Department of Biological Sciences, Purdue University, West Lafayette, IN 47907

Correspondence to D.F. Ready: dready{at}bilbo.bio.purdue.edu

Sensory neuron terminal differentiation tasks apical secretory transport with delivery of abundant biosynthetic traffic to the growing sensory membrane. We recently showed Drosophila Rab11 is essential for rhodopsin transport in developing photoreceptors and asked here if myosin V and the Drosophila Rab11 interacting protein, dRip11, also participate in secretory transport. Reduction of either protein impaired rhodopsin transport, stunting rhabdomere growth and promoting accumulation of cytoplasmic rhodopsin. MyoV-reduced photoreceptors also developed ectopic rhabdomeres inappropriately located in basolateral membrane, indicating a role for MyoV in photoreceptor polarity. Binary yeast two hybrids and in vitro protein–protein interaction predict a ternary complex assembled by independent dRip11 and MyoV binding to Rab11. We propose this complex delivers morphogenic secretory traffic along polarized actin filaments of the subcortical terminal web to the exocytic plasma membrane target, the rhabdomere base. A protein trio conserved across eukaryotes thus mediates normal, in vivo sensory neuron morphogenesis.

B.X. Li and A.K. Satoh contributed equally to this paper.

Abbreviations used in this paper: FIP, family interacting protein; MyoV, myosin V; RBD, Rab11 binding domain; Rh1, rhodopsin1; RTW, rhabdomere terminal web.


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