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

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...

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Autores principales: Chorna-Ornan, Irit, Tzarfaty, Vered, Ankri-Eliahoo, Galit, Joel-Almagor, Tamar, Meyer, Nina E., Huber, Armin, Payre, François, Minke, Baruch
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1936436/
https://www.ncbi.nlm.nih.gov/pubmed/16216927
http://dx.doi.org/10.1083/jcb.200503014
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author Chorna-Ornan, Irit
Tzarfaty, Vered
Ankri-Eliahoo, Galit
Joel-Almagor, Tamar
Meyer, Nina E.
Huber, Armin
Payre, François
Minke, Baruch
author_facet Chorna-Ornan, Irit
Tzarfaty, Vered
Ankri-Eliahoo, Galit
Joel-Almagor, Tamar
Meyer, Nina E.
Huber, Armin
Payre, François
Minke, Baruch
author_sort Chorna-Ornan, Irit
collection PubMed
description 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.
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spelling pubmed-19364362008-03-05 Light-regulated interaction of Dmoesin with TRP and TRPL channels is required for maintenance of photoreceptors Chorna-Ornan, Irit Tzarfaty, Vered Ankri-Eliahoo, Galit Joel-Almagor, Tamar Meyer, Nina E. Huber, Armin Payre, François Minke, Baruch J Cell Biol Research Articles 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. The Rockefeller University Press 2005-10-10 /pmc/articles/PMC1936436/ /pubmed/16216927 http://dx.doi.org/10.1083/jcb.200503014 Text en Copyright © 2005, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Research Articles
Chorna-Ornan, Irit
Tzarfaty, Vered
Ankri-Eliahoo, Galit
Joel-Almagor, Tamar
Meyer, Nina E.
Huber, Armin
Payre, François
Minke, Baruch
Light-regulated interaction of Dmoesin with TRP and TRPL channels is required for maintenance of photoreceptors
title Light-regulated interaction of Dmoesin with TRP and TRPL channels is required for maintenance of photoreceptors
title_full Light-regulated interaction of Dmoesin with TRP and TRPL channels is required for maintenance of photoreceptors
title_fullStr Light-regulated interaction of Dmoesin with TRP and TRPL channels is required for maintenance of photoreceptors
title_full_unstemmed Light-regulated interaction of Dmoesin with TRP and TRPL channels is required for maintenance of photoreceptors
title_short Light-regulated interaction of Dmoesin with TRP and TRPL channels is required for maintenance of photoreceptors
title_sort light-regulated interaction of dmoesin with trp and trpl channels is required for maintenance of photoreceptors
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1936436/
https://www.ncbi.nlm.nih.gov/pubmed/16216927
http://dx.doi.org/10.1083/jcb.200503014
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