Melanopsin-expressing amphioxus photoreceptors transduce light via a phospholipase C signaling cascade.

Melanopsin, the receptor molecule that underlies light sensitivity in mammalian 'circadian' receptors, is homologous to invertebrate rhodopsins and has been proposed to operate via a similar signaling pathway. Its downstream effectors, however, remain elusive. Melanopsin also expresses in...

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Autores principales:	Juan Manuel Angueyra, Camila Pulido, Gerardo Malagón, Enrico Nasi, Maria Del Pilar Gomez
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/1e0fdf50b1c445deb24aa43cccc60a6f
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spelling	oai:doaj.org-article:1e0fdf50b1c445deb24aa43cccc60a6f2021-11-18T07:31:03ZMelanopsin-expressing amphioxus photoreceptors transduce light via a phospholipase C signaling cascade.1932-620310.1371/journal.pone.0029813https://doaj.org/article/1e0fdf50b1c445deb24aa43cccc60a6f2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22235344/?tool=EBIhttps://doaj.org/toc/1932-6203Melanopsin, the receptor molecule that underlies light sensitivity in mammalian 'circadian' receptors, is homologous to invertebrate rhodopsins and has been proposed to operate via a similar signaling pathway. Its downstream effectors, however, remain elusive. Melanopsin also expresses in two distinct light-sensitive cell types in the neural tube of amphioxus. This organism is the most basal extant chordate and can help outline the evolutionary history of different photoreceptor lineages and their transduction mechanisms; moreover, isolated amphioxus photoreceptors offer unique advantages, because they are unambiguously identifiable and amenable to single-cell physiological assays. In the present study whole-cell patch clamp recording, pharmacological manipulations, and immunodetection were utilized to investigate light transduction in amphioxus photoreceptors. A G(q) was identified and selectively localized to the photosensitive microvillar membrane, while the pivotal role of phospholipase C was established pharmacologically. The photocurrent was profoundly depressed by IP₃ receptor antagonists, highlighting the importance of IP₃ receptors in light signaling. By contrast, surrogates of diacylglycerol (DAG), as well as poly-unsaturated fatty acids failed to activate a membrane conductance or to alter the light response. The results strengthen the notion that calcium released from the ER via IP₃-sensitive channels may fulfill a key role in conveying--directly or indirectly--the melanopsin-initiated light signal to the photoconductance; moreover, they challenge the dogma that microvillar photoreceptors and phoshoinositide-based light transduction are a prerogative of invertebrate eyes.Juan Manuel AngueyraCamila PulidoGerardo MalagónEnrico NasiMaria Del Pilar GomezPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 1, p e29813 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Juan Manuel Angueyra Camila Pulido Gerardo Malagón Enrico Nasi Maria Del Pilar Gomez Melanopsin-expressing amphioxus photoreceptors transduce light via a phospholipase C signaling cascade.
description	Melanopsin, the receptor molecule that underlies light sensitivity in mammalian 'circadian' receptors, is homologous to invertebrate rhodopsins and has been proposed to operate via a similar signaling pathway. Its downstream effectors, however, remain elusive. Melanopsin also expresses in two distinct light-sensitive cell types in the neural tube of amphioxus. This organism is the most basal extant chordate and can help outline the evolutionary history of different photoreceptor lineages and their transduction mechanisms; moreover, isolated amphioxus photoreceptors offer unique advantages, because they are unambiguously identifiable and amenable to single-cell physiological assays. In the present study whole-cell patch clamp recording, pharmacological manipulations, and immunodetection were utilized to investigate light transduction in amphioxus photoreceptors. A G(q) was identified and selectively localized to the photosensitive microvillar membrane, while the pivotal role of phospholipase C was established pharmacologically. The photocurrent was profoundly depressed by IP₃ receptor antagonists, highlighting the importance of IP₃ receptors in light signaling. By contrast, surrogates of diacylglycerol (DAG), as well as poly-unsaturated fatty acids failed to activate a membrane conductance or to alter the light response. The results strengthen the notion that calcium released from the ER via IP₃-sensitive channels may fulfill a key role in conveying--directly or indirectly--the melanopsin-initiated light signal to the photoconductance; moreover, they challenge the dogma that microvillar photoreceptors and phoshoinositide-based light transduction are a prerogative of invertebrate eyes.
format	article
author	Juan Manuel Angueyra Camila Pulido Gerardo Malagón Enrico Nasi Maria Del Pilar Gomez
author_facet	Juan Manuel Angueyra Camila Pulido Gerardo Malagón Enrico Nasi Maria Del Pilar Gomez
author_sort	Juan Manuel Angueyra
title	Melanopsin-expressing amphioxus photoreceptors transduce light via a phospholipase C signaling cascade.
title_short	Melanopsin-expressing amphioxus photoreceptors transduce light via a phospholipase C signaling cascade.
title_full	Melanopsin-expressing amphioxus photoreceptors transduce light via a phospholipase C signaling cascade.
title_fullStr	Melanopsin-expressing amphioxus photoreceptors transduce light via a phospholipase C signaling cascade.
title_full_unstemmed	Melanopsin-expressing amphioxus photoreceptors transduce light via a phospholipase C signaling cascade.
title_sort	melanopsin-expressing amphioxus photoreceptors transduce light via a phospholipase c signaling cascade.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/1e0fdf50b1c445deb24aa43cccc60a6f
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Melanopsin-expressing amphioxus photoreceptors transduce light via a phospholipase C signaling cascade.

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