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Functional analysis in a model sea anemone reveals phylogenetic complexity and a role in cnidocyte discharge of DEG/ENaC ion channels
Ion channels of the DEG/ENaC family share a similar structure but serve strikingly diverse biological functions, such as Na(+) reabsorption, mechanosensing, proton-sensing, chemosensing and cell-cell communication via neuropeptides. This functional diversity raises the question of the ancient functi...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9822975/ https://www.ncbi.nlm.nih.gov/pubmed/36609696 http://dx.doi.org/10.1038/s42003-022-04399-1 |
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author | Aguilar-Camacho, Jose Maria Foreman, Katharina Jaimes-Becerra, Adrian Aharoni, Reuven Gründer, Stefan Moran, Yehu |
author_facet | Aguilar-Camacho, Jose Maria Foreman, Katharina Jaimes-Becerra, Adrian Aharoni, Reuven Gründer, Stefan Moran, Yehu |
author_sort | Aguilar-Camacho, Jose Maria |
collection | PubMed |
description | Ion channels of the DEG/ENaC family share a similar structure but serve strikingly diverse biological functions, such as Na(+) reabsorption, mechanosensing, proton-sensing, chemosensing and cell-cell communication via neuropeptides. This functional diversity raises the question of the ancient function of DEG/ENaCs. Using an extensive phylogenetic analysis across many different animal groups, we found a surprising diversity of DEG/ENaCs already in Cnidaria (corals, sea anemones, hydroids and jellyfish). Using a combination of gene expression analysis, electrophysiological and functional studies combined with pharmacological inhibition as well as genetic knockout in the model cnidarian Nematostella vectensis, we reveal an unanticipated role for a proton-sensitive DEG/ENaC in discharge of N. vectensis cnidocytes, the stinging cells typifying all cnidarians. Our study supports the view that DEG/ENaCs are versatile channels that have been co-opted for diverse functions since their early occurrence in animals and that respond to simple and ancient stimuli, such as omnipresent protons. |
format | Online Article Text |
id | pubmed-9822975 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-98229752023-01-08 Functional analysis in a model sea anemone reveals phylogenetic complexity and a role in cnidocyte discharge of DEG/ENaC ion channels Aguilar-Camacho, Jose Maria Foreman, Katharina Jaimes-Becerra, Adrian Aharoni, Reuven Gründer, Stefan Moran, Yehu Commun Biol Article Ion channels of the DEG/ENaC family share a similar structure but serve strikingly diverse biological functions, such as Na(+) reabsorption, mechanosensing, proton-sensing, chemosensing and cell-cell communication via neuropeptides. This functional diversity raises the question of the ancient function of DEG/ENaCs. Using an extensive phylogenetic analysis across many different animal groups, we found a surprising diversity of DEG/ENaCs already in Cnidaria (corals, sea anemones, hydroids and jellyfish). Using a combination of gene expression analysis, electrophysiological and functional studies combined with pharmacological inhibition as well as genetic knockout in the model cnidarian Nematostella vectensis, we reveal an unanticipated role for a proton-sensitive DEG/ENaC in discharge of N. vectensis cnidocytes, the stinging cells typifying all cnidarians. Our study supports the view that DEG/ENaCs are versatile channels that have been co-opted for diverse functions since their early occurrence in animals and that respond to simple and ancient stimuli, such as omnipresent protons. Nature Publishing Group UK 2023-01-06 /pmc/articles/PMC9822975/ /pubmed/36609696 http://dx.doi.org/10.1038/s42003-022-04399-1 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Aguilar-Camacho, Jose Maria Foreman, Katharina Jaimes-Becerra, Adrian Aharoni, Reuven Gründer, Stefan Moran, Yehu Functional analysis in a model sea anemone reveals phylogenetic complexity and a role in cnidocyte discharge of DEG/ENaC ion channels |
title | Functional analysis in a model sea anemone reveals phylogenetic complexity and a role in cnidocyte discharge of DEG/ENaC ion channels |
title_full | Functional analysis in a model sea anemone reveals phylogenetic complexity and a role in cnidocyte discharge of DEG/ENaC ion channels |
title_fullStr | Functional analysis in a model sea anemone reveals phylogenetic complexity and a role in cnidocyte discharge of DEG/ENaC ion channels |
title_full_unstemmed | Functional analysis in a model sea anemone reveals phylogenetic complexity and a role in cnidocyte discharge of DEG/ENaC ion channels |
title_short | Functional analysis in a model sea anemone reveals phylogenetic complexity and a role in cnidocyte discharge of DEG/ENaC ion channels |
title_sort | functional analysis in a model sea anemone reveals phylogenetic complexity and a role in cnidocyte discharge of deg/enac ion channels |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9822975/ https://www.ncbi.nlm.nih.gov/pubmed/36609696 http://dx.doi.org/10.1038/s42003-022-04399-1 |
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