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Control of protein translation by IP(3)R-mediated Ca(2+) release in Drosophila neuroendocrine cells

The inositol 1,4,5-trisphosphate receptor (IP(3)R) is one of two Ca(2+) channels that gates Ca(2+) release from ER-stores. The ligand IP(3), generated upon specific G-protein coupled receptor activation, binds to IP(3)R to release Ca(2+) into the cytosol. IP(3)R also mediates ER-store Ca(2+) release...

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Detalles Bibliográficos
Autores principales: Megha,  , Hasan, Gaiti
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5721944/
https://www.ncbi.nlm.nih.gov/pubmed/28949794
http://dx.doi.org/10.1080/19336934.2017.1384103
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author Megha,  
Hasan, Gaiti
author_facet Megha,  
Hasan, Gaiti
author_sort Megha,  
collection PubMed
description The inositol 1,4,5-trisphosphate receptor (IP(3)R) is one of two Ca(2+) channels that gates Ca(2+) release from ER-stores. The ligand IP(3), generated upon specific G-protein coupled receptor activation, binds to IP(3)R to release Ca(2+) into the cytosol. IP(3)R also mediates ER-store Ca(2+) release into the mitochondria, under basal as well as stimulatory conditions; an activity that influences cellular bioenergetics and thus, cellular growth and proliferation. In Drosophila neuroendocrine cells expressing a hypomorphic mutant of IP(3)R, we observed reduced protein translation levels. Here, we discuss the possible molecular mechanism for this observation. We hypothesize that the cellular energy sensor, AMPK connects IP(3)R mediated Ca(2+) release into the mitochondria, to protein translation, via the TOR pathway.
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spelling pubmed-57219442017-12-13 Control of protein translation by IP(3)R-mediated Ca(2+) release in Drosophila neuroendocrine cells Megha,   Hasan, Gaiti Fly (Austin) Extra View The inositol 1,4,5-trisphosphate receptor (IP(3)R) is one of two Ca(2+) channels that gates Ca(2+) release from ER-stores. The ligand IP(3), generated upon specific G-protein coupled receptor activation, binds to IP(3)R to release Ca(2+) into the cytosol. IP(3)R also mediates ER-store Ca(2+) release into the mitochondria, under basal as well as stimulatory conditions; an activity that influences cellular bioenergetics and thus, cellular growth and proliferation. In Drosophila neuroendocrine cells expressing a hypomorphic mutant of IP(3)R, we observed reduced protein translation levels. Here, we discuss the possible molecular mechanism for this observation. We hypothesize that the cellular energy sensor, AMPK connects IP(3)R mediated Ca(2+) release into the mitochondria, to protein translation, via the TOR pathway. Taylor & Francis 2017-09-26 /pmc/articles/PMC5721944/ /pubmed/28949794 http://dx.doi.org/10.1080/19336934.2017.1384103 Text en © 2017 The Author(s). Published with license by Taylor & Francis http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.
spellingShingle Extra View
Megha,  
Hasan, Gaiti
Control of protein translation by IP(3)R-mediated Ca(2+) release in Drosophila neuroendocrine cells
title Control of protein translation by IP(3)R-mediated Ca(2+) release in Drosophila neuroendocrine cells
title_full Control of protein translation by IP(3)R-mediated Ca(2+) release in Drosophila neuroendocrine cells
title_fullStr Control of protein translation by IP(3)R-mediated Ca(2+) release in Drosophila neuroendocrine cells
title_full_unstemmed Control of protein translation by IP(3)R-mediated Ca(2+) release in Drosophila neuroendocrine cells
title_short Control of protein translation by IP(3)R-mediated Ca(2+) release in Drosophila neuroendocrine cells
title_sort control of protein translation by ip(3)r-mediated ca(2+) release in drosophila neuroendocrine cells
topic Extra View
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5721944/
https://www.ncbi.nlm.nih.gov/pubmed/28949794
http://dx.doi.org/10.1080/19336934.2017.1384103
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