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Conservation of estrogen receptor function in invertebrate reproduction
BACKGROUND: Rotifers are microscopic aquatic invertebrates that reproduce both sexually and asexually. Though rotifers are phylogenetically distant from humans, and have specialized reproductive physiology, this work identifies a surprising conservation in the control of reproduction between humans...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5336670/ https://www.ncbi.nlm.nih.gov/pubmed/28259146 http://dx.doi.org/10.1186/s12862-017-0909-z |
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author | Jones, Brande L. Walker, Chris Azizi, Bahareh Tolbert, Laren Williams, Loren Dean Snell, Terry W. |
author_facet | Jones, Brande L. Walker, Chris Azizi, Bahareh Tolbert, Laren Williams, Loren Dean Snell, Terry W. |
author_sort | Jones, Brande L. |
collection | PubMed |
description | BACKGROUND: Rotifers are microscopic aquatic invertebrates that reproduce both sexually and asexually. Though rotifers are phylogenetically distant from humans, and have specialized reproductive physiology, this work identifies a surprising conservation in the control of reproduction between humans and rotifers through the estrogen receptor. Until recently, steroid signaling has been observed in only a few invertebrate taxa and its role in regulating invertebrate reproduction has not been clearly demonstrated. Insights into the evolution of sex signaling pathways can be gained by clarifying how receptors function in invertebrate reproduction. RESULTS: In this paper, we show that a ligand-activated estrogen-like receptor in rotifers binds human estradiol and regulates reproductive output in females. In other invertebrates characterized thus far, ER ligand binding domains have occluded ligand-binding sites and the ERs are not ligand activated. We have used a suite of computational, biochemical and biological techniques to determine that the rotifer ER binding site is not occluded and can bind human estradiol. CONCLUSIONS: Our results demonstrate that this mammalian hormone receptor plays a key role in reproduction of the ancient microinvertebrate Brachinous manjavacas. The presence and activity of the ER within the phylum Rotifera indicates that the ER structure and function is highly conserved throughout animal evolution. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12862-017-0909-z) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5336670 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-53366702017-03-07 Conservation of estrogen receptor function in invertebrate reproduction Jones, Brande L. Walker, Chris Azizi, Bahareh Tolbert, Laren Williams, Loren Dean Snell, Terry W. BMC Evol Biol Research Article BACKGROUND: Rotifers are microscopic aquatic invertebrates that reproduce both sexually and asexually. Though rotifers are phylogenetically distant from humans, and have specialized reproductive physiology, this work identifies a surprising conservation in the control of reproduction between humans and rotifers through the estrogen receptor. Until recently, steroid signaling has been observed in only a few invertebrate taxa and its role in regulating invertebrate reproduction has not been clearly demonstrated. Insights into the evolution of sex signaling pathways can be gained by clarifying how receptors function in invertebrate reproduction. RESULTS: In this paper, we show that a ligand-activated estrogen-like receptor in rotifers binds human estradiol and regulates reproductive output in females. In other invertebrates characterized thus far, ER ligand binding domains have occluded ligand-binding sites and the ERs are not ligand activated. We have used a suite of computational, biochemical and biological techniques to determine that the rotifer ER binding site is not occluded and can bind human estradiol. CONCLUSIONS: Our results demonstrate that this mammalian hormone receptor plays a key role in reproduction of the ancient microinvertebrate Brachinous manjavacas. The presence and activity of the ER within the phylum Rotifera indicates that the ER structure and function is highly conserved throughout animal evolution. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12862-017-0909-z) contains supplementary material, which is available to authorized users. BioMed Central 2017-03-04 /pmc/articles/PMC5336670/ /pubmed/28259146 http://dx.doi.org/10.1186/s12862-017-0909-z Text en © The Author(s). 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Jones, Brande L. Walker, Chris Azizi, Bahareh Tolbert, Laren Williams, Loren Dean Snell, Terry W. Conservation of estrogen receptor function in invertebrate reproduction |
title | Conservation of estrogen receptor function in invertebrate reproduction |
title_full | Conservation of estrogen receptor function in invertebrate reproduction |
title_fullStr | Conservation of estrogen receptor function in invertebrate reproduction |
title_full_unstemmed | Conservation of estrogen receptor function in invertebrate reproduction |
title_short | Conservation of estrogen receptor function in invertebrate reproduction |
title_sort | conservation of estrogen receptor function in invertebrate reproduction |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5336670/ https://www.ncbi.nlm.nih.gov/pubmed/28259146 http://dx.doi.org/10.1186/s12862-017-0909-z |
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