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Main Authors: Zahnow, Fynn, Jäger, Chiara, Mohamed, Yassmin, Vogelhuber, Gianluca, May, Fabian, Ciocan, Alexandra Maria, Manieri, Arianna, Maxeiner, Stephan, Krasteva-Christ, Gabriela, Cobain, Matthew R D, Podsiadlowski, Lars, Crespo-Picazo, José Luis, García-Párraga, Daniel, Althaus, Mike
Format: Artículo científico
Language:en
Published: bioRxiv : the preprint server for biology 2024
Online Access:https://pubmed.ncbi.nlm.nih.gov/39605611/
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author Zahnow, Fynn
Jäger, Chiara
Mohamed, Yassmin
Vogelhuber, Gianluca
May, Fabian
Ciocan, Alexandra Maria
Manieri, Arianna
Maxeiner, Stephan
Krasteva-Christ, Gabriela
Cobain, Matthew R D
Podsiadlowski, Lars
Crespo-Picazo, José Luis
García-Párraga, Daniel
Althaus, Mike
author_facet Zahnow, Fynn
Jäger, Chiara
Mohamed, Yassmin
Vogelhuber, Gianluca
May, Fabian
Ciocan, Alexandra Maria
Manieri, Arianna
Maxeiner, Stephan
Krasteva-Christ, Gabriela
Cobain, Matthew R D
Podsiadlowski, Lars
Crespo-Picazo, José Luis
García-Párraga, Daniel
Althaus, Mike
Zahnow, Fynn
Jäger, Chiara
Mohamed, Yassmin
Vogelhuber, Gianluca
May, Fabian
Ciocan, Alexandra Maria
Manieri, Arianna
Maxeiner, Stephan
Krasteva-Christ, Gabriela
Cobain, Matthew R D
Podsiadlowski, Lars
Crespo-Picazo, José Luis
García-Párraga, Daniel
Althaus, Mike
collection PubMed - marine biology
contents The evolutionary path of the epithelial sodium channel δ-subunit in Cetartiodactyla points to a role in sodium sensing. Zahnow, Fynn Jäger, Chiara Mohamed, Yassmin Vogelhuber, Gianluca May, Fabian Ciocan, Alexandra Maria Manieri, Arianna Maxeiner, Stephan Krasteva-Christ, Gabriela Cobain, Matthew R D Podsiadlowski, Lars Crespo-Picazo, José Luis García-Párraga, Daniel Althaus, Mike The epithelial sodium channel (ENaC) plays a key role in osmoregulation in tetrapod vertebrates and is a candidate receptor for salt taste sensation. There are four ENaC subunits (α, β, γ, δ) which form αβγ- or δβγ ENaCs. While αβγ-ENaC is a 'maintenance protein' controlling sodium and potassium homeostasis, δβγ-ENaC might represent a 'stress protein' monitoring high sodium concentrations. The δ-subunit emerged with water-to-land transition of tetrapod vertebrate ancestors. We investigated the evolutionary path of ENaC-coding genes in Cetartiodactyla, a group comprising even-toed ungulates and the cetaceans (whales/dolphins) which transitioned from terrestrial to marine environments in the Eocene. The genes (α-ENaC), (β-ENaC) and (γ-ENaC) are intact in all 22 investigated cetartiodactylan families. While (δ-ENaC) is intact in terrestrial Artiodactyla, it is a pseudogene in 12 cetacean families. A fusion of exons 11 and 12 under preservation of the open reading frame was observed in the Antilopinae, representing a new feature of this clade. Transcripts of and were present in kidney and lung tissues of Bottlenose dolphins, highlighting αβγ-ENaC's role as a maintenance protein. Consistent with loss, Bottlenose dolphins and Beluga whales did not show behavioural differences to stimuli with or without sodium in seawater-equivalent concentrations. These data suggest a function of δ-ENaC as a sodium sensing protein which might have become obsolete in cetaceans after the migration to high-salinity marine environments. Consistently, there is reduced selection pressure or pseudogenisation of in other marine mammals, including sirenians, pinnipeds and sea otter.
format Artículo científico
id pubmed_39605611
institution PubMed
language en
publishDate 2024
publisher bioRxiv : the preprint server for biology
record_format pubmed
spellingShingle The evolutionary path of the epithelial sodium channel δ-subunit in Cetartiodactyla points to a role in sodium sensing.
Zahnow, Fynn
Jäger, Chiara
Mohamed, Yassmin
Vogelhuber, Gianluca
May, Fabian
Ciocan, Alexandra Maria
Manieri, Arianna
Maxeiner, Stephan
Krasteva-Christ, Gabriela
Cobain, Matthew R D
Podsiadlowski, Lars
Crespo-Picazo, José Luis
García-Párraga, Daniel
Althaus, Mike
The evolutionary path of the epithelial sodium channel δ-subunit in Cetartiodactyla points to a role in sodium sensing. Zahnow, Fynn Jäger, Chiara Mohamed, Yassmin Vogelhuber, Gianluca May, Fabian Ciocan, Alexandra Maria Manieri, Arianna Maxeiner, Stephan Krasteva-Christ, Gabriela Cobain, Matthew R D Podsiadlowski, Lars Crespo-Picazo, José Luis García-Párraga, Daniel Althaus, Mike The epithelial sodium channel (ENaC) plays a key role in osmoregulation in tetrapod vertebrates and is a candidate receptor for salt taste sensation. There are four ENaC subunits (α, β, γ, δ) which form αβγ- or δβγ ENaCs. While αβγ-ENaC is a 'maintenance protein' controlling sodium and potassium homeostasis, δβγ-ENaC might represent a 'stress protein' monitoring high sodium concentrations. The δ-subunit emerged with water-to-land transition of tetrapod vertebrate ancestors. We investigated the evolutionary path of ENaC-coding genes in Cetartiodactyla, a group comprising even-toed ungulates and the cetaceans (whales/dolphins) which transitioned from terrestrial to marine environments in the Eocene. The genes (α-ENaC), (β-ENaC) and (γ-ENaC) are intact in all 22 investigated cetartiodactylan families. While (δ-ENaC) is intact in terrestrial Artiodactyla, it is a pseudogene in 12 cetacean families. A fusion of exons 11 and 12 under preservation of the open reading frame was observed in the Antilopinae, representing a new feature of this clade. Transcripts of and were present in kidney and lung tissues of Bottlenose dolphins, highlighting αβγ-ENaC's role as a maintenance protein. Consistent with loss, Bottlenose dolphins and Beluga whales did not show behavioural differences to stimuli with or without sodium in seawater-equivalent concentrations. These data suggest a function of δ-ENaC as a sodium sensing protein which might have become obsolete in cetaceans after the migration to high-salinity marine environments. Consistently, there is reduced selection pressure or pseudogenisation of in other marine mammals, including sirenians, pinnipeds and sea otter.
title The evolutionary path of the epithelial sodium channel δ-subunit in Cetartiodactyla points to a role in sodium sensing.
url https://pubmed.ncbi.nlm.nih.gov/39605611/