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Agonist-mediated assembly of the crustacean methyl farnesoate receptor

The methyl farnesoate receptor (MfR) orchestrates aspects of reproduction and development such as male sex determination in branchiopod crustaceans. Phenotypic endpoints regulated by the receptor have been well-documented, but molecular interactions involved in receptor activation remain elusive. We...

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Autores principales: Kakaley, Elizabeth K. Medlock, Wang, Helen Y., LeBlanc, Gerald A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5359607/
https://www.ncbi.nlm.nih.gov/pubmed/28322350
http://dx.doi.org/10.1038/srep45071
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author Kakaley, Elizabeth K. Medlock
Wang, Helen Y.
LeBlanc, Gerald A.
author_facet Kakaley, Elizabeth K. Medlock
Wang, Helen Y.
LeBlanc, Gerald A.
author_sort Kakaley, Elizabeth K. Medlock
collection PubMed
description The methyl farnesoate receptor (MfR) orchestrates aspects of reproduction and development such as male sex determination in branchiopod crustaceans. Phenotypic endpoints regulated by the receptor have been well-documented, but molecular interactions involved in receptor activation remain elusive. We hypothesized that the MfR subunits, methoprene-tolerant transcription factor (Met) and steroid receptor coactivator (SRC), would be expressed coincident with the timing of sex programming of developing oocytes by methyl farnesoate in daphnids. We also hypothesized that methyl farnesoate activates MfR assembly. Met mRNA was expressed rhythmically during the reproductive cycle, with peak mRNA accumulation just prior period of oocytes programming of sex. Further, we revealed evidence that Met proteins self-associate in the absence of methyl farnesoate, and that the presence of methyl farnesoate stimulates dissociation of Met multimers with subsequent association with SRC. Results demonstrated that the Met subunit is highly dynamic in controlling the action of methyl farnesoate through temporal variation in its expression and availability for receptor assembly.
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spelling pubmed-53596072017-03-22 Agonist-mediated assembly of the crustacean methyl farnesoate receptor Kakaley, Elizabeth K. Medlock Wang, Helen Y. LeBlanc, Gerald A. Sci Rep Article The methyl farnesoate receptor (MfR) orchestrates aspects of reproduction and development such as male sex determination in branchiopod crustaceans. Phenotypic endpoints regulated by the receptor have been well-documented, but molecular interactions involved in receptor activation remain elusive. We hypothesized that the MfR subunits, methoprene-tolerant transcription factor (Met) and steroid receptor coactivator (SRC), would be expressed coincident with the timing of sex programming of developing oocytes by methyl farnesoate in daphnids. We also hypothesized that methyl farnesoate activates MfR assembly. Met mRNA was expressed rhythmically during the reproductive cycle, with peak mRNA accumulation just prior period of oocytes programming of sex. Further, we revealed evidence that Met proteins self-associate in the absence of methyl farnesoate, and that the presence of methyl farnesoate stimulates dissociation of Met multimers with subsequent association with SRC. Results demonstrated that the Met subunit is highly dynamic in controlling the action of methyl farnesoate through temporal variation in its expression and availability for receptor assembly. Nature Publishing Group 2017-03-21 /pmc/articles/PMC5359607/ /pubmed/28322350 http://dx.doi.org/10.1038/srep45071 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Kakaley, Elizabeth K. Medlock
Wang, Helen Y.
LeBlanc, Gerald A.
Agonist-mediated assembly of the crustacean methyl farnesoate receptor
title Agonist-mediated assembly of the crustacean methyl farnesoate receptor
title_full Agonist-mediated assembly of the crustacean methyl farnesoate receptor
title_fullStr Agonist-mediated assembly of the crustacean methyl farnesoate receptor
title_full_unstemmed Agonist-mediated assembly of the crustacean methyl farnesoate receptor
title_short Agonist-mediated assembly of the crustacean methyl farnesoate receptor
title_sort agonist-mediated assembly of the crustacean methyl farnesoate receptor
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5359607/
https://www.ncbi.nlm.nih.gov/pubmed/28322350
http://dx.doi.org/10.1038/srep45071
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