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Published 10 October 2005. doi:10.1083/jcb.200503014
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 1, 143-152
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Article

Light-regulated interaction of Dmoesin with TRP and TRPL channels is required for maintenance of photoreceptors



Irit Chorna-Ornan1,2, Vered Tzarfaty1,2, Galit Ankri-Eliahoo1,2, Tamar Joel-Almagor1,2, Nina E. Meyer3, Armin Huber3, François Payre4, and Baruch Minke1,2

1 Department of Physiology, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel
2 the Kühne Minerva Center for Studies of Visual Transduction, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel
3 Department of Cell Biology and Neurobiology, Zoological Institute, University of Karlsruhe, 76131 Karlsruhe, Germany
4 Centre de Biologie du Développement, Université Paul Sabatier, 31062 Cedex 4, Toulouse, France

Correspondence to Baruch Minke: minke{at}md.huji.ac.il

Recent studies in Drosophila melanogaster retina indicate that absorption of light causes the translocation of signaling molecules and actin from the photoreceptor's signaling membrane to the cytosol, but the underlying mechanisms are not fully understood. As ezrin-radixin-moesin (ERM) proteins are known to regulate actin–membrane interactions in a signal-dependent manner, we analyzed the role of Dmoesin, the unique D. melanogaster ERM, in response to light. We report that the illumination of dark-raised flies triggers the dissociation of Dmoesin from the light-sensitive transient receptor potential (TRP) and TRP-like channels, followed by the migration of Dmoesin from the membrane to the cytoplasm. Furthermore, we show that light-activated migration of Dmoesin results from the dephosphorylation of a conserved threonine in Dmoesin. The expression of a Dmoesin mutant form that impairs this phosphorylation inhibits Dmoesin movement and leads to light-induced retinal degeneration. Thus, our data strongly suggest that the light- and phosphorylation-dependent dynamic association of Dmoesin to membrane channels is involved in maintenance of the photoreceptor cells.

I. Chorna-Ornan and V. Tzarfaty contributed equally to this paper.

Abbreviations used in this paper: EBP50, ezrin binding phosphoprotein 50; ERM, ezrin-radixin-moesin; INAD, inactivation-no-afterpotential D; NIS, nonimmune serum; PDZ, PSD95/DlgA/ZO-1 homology; PIP2, phosphatidylinositol 4,5-bisphosphate; T559, threonine 559; TRP, transient receptor potential; TRPL, TRP-like; WT, wild-type.


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