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Contributions of UBE2C and UBE2S to meiotic progression of porcine oocytes

Vertebrate oocytes arrested at the first meiotic prophase must proceed to the second meiotic metaphase (MII) before fertilization. This meiotic process requires the precise control of protein degradation. Part of the protein degradation in oocytes is controlled by members of the ubiquitin-conjugatin...

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Autores principales: FUJIOKA, Yoshie A., ONUMA, Asuka, FUJII, Wataru, SUGIURA, Koji, NAITO, Kunihiko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Society for Reproduction and Development 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6021604/
https://www.ncbi.nlm.nih.gov/pubmed/29576589
http://dx.doi.org/10.1262/jrd.2018-006
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author FUJIOKA, Yoshie A.
ONUMA, Asuka
FUJII, Wataru
SUGIURA, Koji
NAITO, Kunihiko
author_facet FUJIOKA, Yoshie A.
ONUMA, Asuka
FUJII, Wataru
SUGIURA, Koji
NAITO, Kunihiko
author_sort FUJIOKA, Yoshie A.
collection PubMed
description Vertebrate oocytes arrested at the first meiotic prophase must proceed to the second meiotic metaphase (MII) before fertilization. This meiotic process requires the precise control of protein degradation. Part of the protein degradation in oocytes is controlled by members of the ubiquitin-conjugating enzyme family, UBE2C and UBE2S, which are known to participate in mono-ubiquitination and poly-ubiquitination, respectively. Although UBE2 enzymes have been well studied in mitosis, their contribution to mammalian oocyte meiosis is relatively unknown and has been studied only in mice. Here, we investigated the contribution of UBE2C and UBE2S to porcine oocyte maturation using an RNA injection method. Overexpression of UBE2S prevented MII arrest of oocytes and led to the formation of a pronucleus (PN) at 48 h of culture. This effect was also observed for prolonged cultures of UBE2C-overexpressing oocytes, suggesting the effectiveness of poly-ubiquitination in the rapid escape from M-phase in porcine oocytes. Although the inhibition of either UBE2C or UBE2S by antisense RNA (asRNA) injection had no effect on oocyte maturation, asRNA-injected oocytes showed inhibited PN formation after parthenogenetic activation. These results indicated that ubiquitination of certain factors by UBE2S and UBE2C plays a role in the escape from MII arrest in porcine oocytes. Further investigations to identify the factors and how mono- and/or poly-ubiquitination contributes to protein degradation could provide a better understanding of UBE2 roles in oocyte maturation.
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spelling pubmed-60216042018-07-05 Contributions of UBE2C and UBE2S to meiotic progression of porcine oocytes FUJIOKA, Yoshie A. ONUMA, Asuka FUJII, Wataru SUGIURA, Koji NAITO, Kunihiko J Reprod Dev Original Article Vertebrate oocytes arrested at the first meiotic prophase must proceed to the second meiotic metaphase (MII) before fertilization. This meiotic process requires the precise control of protein degradation. Part of the protein degradation in oocytes is controlled by members of the ubiquitin-conjugating enzyme family, UBE2C and UBE2S, which are known to participate in mono-ubiquitination and poly-ubiquitination, respectively. Although UBE2 enzymes have been well studied in mitosis, their contribution to mammalian oocyte meiosis is relatively unknown and has been studied only in mice. Here, we investigated the contribution of UBE2C and UBE2S to porcine oocyte maturation using an RNA injection method. Overexpression of UBE2S prevented MII arrest of oocytes and led to the formation of a pronucleus (PN) at 48 h of culture. This effect was also observed for prolonged cultures of UBE2C-overexpressing oocytes, suggesting the effectiveness of poly-ubiquitination in the rapid escape from M-phase in porcine oocytes. Although the inhibition of either UBE2C or UBE2S by antisense RNA (asRNA) injection had no effect on oocyte maturation, asRNA-injected oocytes showed inhibited PN formation after parthenogenetic activation. These results indicated that ubiquitination of certain factors by UBE2S and UBE2C plays a role in the escape from MII arrest in porcine oocytes. Further investigations to identify the factors and how mono- and/or poly-ubiquitination contributes to protein degradation could provide a better understanding of UBE2 roles in oocyte maturation. The Society for Reproduction and Development 2018-03-23 2018-06 /pmc/articles/PMC6021604/ /pubmed/29576589 http://dx.doi.org/10.1262/jrd.2018-006 Text en ©2018 Society for Reproduction and Development This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial No Derivatives (by-nc-nd) License. (CC-BY-NC-ND 4.0: https://creativecommons.org/licenses/by-nc-nd/4.0/)
spellingShingle Original Article
FUJIOKA, Yoshie A.
ONUMA, Asuka
FUJII, Wataru
SUGIURA, Koji
NAITO, Kunihiko
Contributions of UBE2C and UBE2S to meiotic progression of porcine oocytes
title Contributions of UBE2C and UBE2S to meiotic progression of porcine oocytes
title_full Contributions of UBE2C and UBE2S to meiotic progression of porcine oocytes
title_fullStr Contributions of UBE2C and UBE2S to meiotic progression of porcine oocytes
title_full_unstemmed Contributions of UBE2C and UBE2S to meiotic progression of porcine oocytes
title_short Contributions of UBE2C and UBE2S to meiotic progression of porcine oocytes
title_sort contributions of ube2c and ube2s to meiotic progression of porcine oocytes
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6021604/
https://www.ncbi.nlm.nih.gov/pubmed/29576589
http://dx.doi.org/10.1262/jrd.2018-006
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