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Identification of New Regulators of the Oocyte-to-Embryo Transition in Drosophila

At the oocyte-to-embryo transition the highly differentiated oocyte arrested in meiosis becomes a totipotent embryo capable of embryogenesis. Oocyte maturation (release of the prophase I primary arrest) and egg activation (release from the secondary meiotic arrest and the trigger for the oocyte-to-e...

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Autores principales: Avilés-Pagán, Emir E., Kang, Albert S. W., Orr-Weaver, Terry L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Genetics Society of America 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7466974/
https://www.ncbi.nlm.nih.gov/pubmed/32690584
http://dx.doi.org/10.1534/g3.120.401415
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author Avilés-Pagán, Emir E.
Kang, Albert S. W.
Orr-Weaver, Terry L.
author_facet Avilés-Pagán, Emir E.
Kang, Albert S. W.
Orr-Weaver, Terry L.
author_sort Avilés-Pagán, Emir E.
collection PubMed
description At the oocyte-to-embryo transition the highly differentiated oocyte arrested in meiosis becomes a totipotent embryo capable of embryogenesis. Oocyte maturation (release of the prophase I primary arrest) and egg activation (release from the secondary meiotic arrest and the trigger for the oocyte-to-embryo transition) serve as prerequisites for this transition, both events being controlled posttranscriptionally. Recently, we obtained a comprehensive list of proteins whose levels are developmentally regulated during these events via a high-throughput quantitative proteomic analysis of Drosophila melanogaster oocyte maturation and egg activation. We conducted a targeted screen for potential novel regulators of the oocyte-to-embryo transition, selecting 53 candidates from these proteins. We reduced the function of each candidate gene using transposable element insertion alleles and RNAi, and screened for defects in oocyte maturation or early embryogenesis. Deletion of the aquaporin gene CG7777 did not affect female fertility. However, we identified CG5003 and nebu (CG10960) as new regulators of the transition from oocyte to embryo. Mutations in CG5003, which encodes an F-box protein associated with SCF-proteasome degradation function, cause a decrease in female fertility and early embryonic arrest. Mutations in nebu, encoding a putative glucose transporter, result in defects during the early embryonic divisions, as well as a developmental delay and arrest. nebu mutants also exhibit a defect in glycogen accumulation during late oogenesis. Our findings highlight potential previously unknown roles for the ubiquitin protein degradation pathway and sugar transport across membranes during this time, and paint a broader picture of the underlying requirements of the oocyte-to-embryo transition.
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spelling pubmed-74669742020-09-14 Identification of New Regulators of the Oocyte-to-Embryo Transition in Drosophila Avilés-Pagán, Emir E. Kang, Albert S. W. Orr-Weaver, Terry L. G3 (Bethesda) Mutant Screen Report At the oocyte-to-embryo transition the highly differentiated oocyte arrested in meiosis becomes a totipotent embryo capable of embryogenesis. Oocyte maturation (release of the prophase I primary arrest) and egg activation (release from the secondary meiotic arrest and the trigger for the oocyte-to-embryo transition) serve as prerequisites for this transition, both events being controlled posttranscriptionally. Recently, we obtained a comprehensive list of proteins whose levels are developmentally regulated during these events via a high-throughput quantitative proteomic analysis of Drosophila melanogaster oocyte maturation and egg activation. We conducted a targeted screen for potential novel regulators of the oocyte-to-embryo transition, selecting 53 candidates from these proteins. We reduced the function of each candidate gene using transposable element insertion alleles and RNAi, and screened for defects in oocyte maturation or early embryogenesis. Deletion of the aquaporin gene CG7777 did not affect female fertility. However, we identified CG5003 and nebu (CG10960) as new regulators of the transition from oocyte to embryo. Mutations in CG5003, which encodes an F-box protein associated with SCF-proteasome degradation function, cause a decrease in female fertility and early embryonic arrest. Mutations in nebu, encoding a putative glucose transporter, result in defects during the early embryonic divisions, as well as a developmental delay and arrest. nebu mutants also exhibit a defect in glycogen accumulation during late oogenesis. Our findings highlight potential previously unknown roles for the ubiquitin protein degradation pathway and sugar transport across membranes during this time, and paint a broader picture of the underlying requirements of the oocyte-to-embryo transition. Genetics Society of America 2020-07-20 /pmc/articles/PMC7466974/ /pubmed/32690584 http://dx.doi.org/10.1534/g3.120.401415 Text en Copyright © 2020 Aviles-Pagan et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article 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 the original work is properly cited.
spellingShingle Mutant Screen Report
Avilés-Pagán, Emir E.
Kang, Albert S. W.
Orr-Weaver, Terry L.
Identification of New Regulators of the Oocyte-to-Embryo Transition in Drosophila
title Identification of New Regulators of the Oocyte-to-Embryo Transition in Drosophila
title_full Identification of New Regulators of the Oocyte-to-Embryo Transition in Drosophila
title_fullStr Identification of New Regulators of the Oocyte-to-Embryo Transition in Drosophila
title_full_unstemmed Identification of New Regulators of the Oocyte-to-Embryo Transition in Drosophila
title_short Identification of New Regulators of the Oocyte-to-Embryo Transition in Drosophila
title_sort identification of new regulators of the oocyte-to-embryo transition in drosophila
topic Mutant Screen Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7466974/
https://www.ncbi.nlm.nih.gov/pubmed/32690584
http://dx.doi.org/10.1534/g3.120.401415
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