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Importance of ERK1/2 in Regulation of Protein Translation during Oocyte Meiosis

Although the involvement of the extracellular signal-regulated kinases 1 and 2 (ERK1/2) pathway in the regulation of cytostatic factor (CSF) activity; as well as in microtubules organization during meiotic maturation of oocytes; has already been described in detail; rather less attention has been pa...

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Detalles Bibliográficos
Autores principales: Kalous, Jaroslav, Tetkova, Anna, Kubelka, Michal, Susor, Andrej
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5877559/
https://www.ncbi.nlm.nih.gov/pubmed/29494492
http://dx.doi.org/10.3390/ijms19030698
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author Kalous, Jaroslav
Tetkova, Anna
Kubelka, Michal
Susor, Andrej
author_facet Kalous, Jaroslav
Tetkova, Anna
Kubelka, Michal
Susor, Andrej
author_sort Kalous, Jaroslav
collection PubMed
description Although the involvement of the extracellular signal-regulated kinases 1 and 2 (ERK1/2) pathway in the regulation of cytostatic factor (CSF) activity; as well as in microtubules organization during meiotic maturation of oocytes; has already been described in detail; rather less attention has been paid to the role of ERK1/2 in the regulation of mRNA translation. However; important data on the role of ERK1/2 in translation during oocyte meiosis have been documented. This review focuses on recent findings regarding the regulation of translation and the role of ERK1/2 in this process in the meiotic cycle of mammalian oocytes. The specific role of ERK1/2 in the regulation of mammalian target of rapamycin (mTOR); eukaryotic translation initiation factor 4E (eIF4E) and cytoplasmic polyadenylation element binding protein 1 (CPEB1) activity is addressed along with additional focus on the other key players involved in protein translation.
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spelling pubmed-58775592018-04-09 Importance of ERK1/2 in Regulation of Protein Translation during Oocyte Meiosis Kalous, Jaroslav Tetkova, Anna Kubelka, Michal Susor, Andrej Int J Mol Sci Review Although the involvement of the extracellular signal-regulated kinases 1 and 2 (ERK1/2) pathway in the regulation of cytostatic factor (CSF) activity; as well as in microtubules organization during meiotic maturation of oocytes; has already been described in detail; rather less attention has been paid to the role of ERK1/2 in the regulation of mRNA translation. However; important data on the role of ERK1/2 in translation during oocyte meiosis have been documented. This review focuses on recent findings regarding the regulation of translation and the role of ERK1/2 in this process in the meiotic cycle of mammalian oocytes. The specific role of ERK1/2 in the regulation of mammalian target of rapamycin (mTOR); eukaryotic translation initiation factor 4E (eIF4E) and cytoplasmic polyadenylation element binding protein 1 (CPEB1) activity is addressed along with additional focus on the other key players involved in protein translation. MDPI 2018-03-01 /pmc/articles/PMC5877559/ /pubmed/29494492 http://dx.doi.org/10.3390/ijms19030698 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Kalous, Jaroslav
Tetkova, Anna
Kubelka, Michal
Susor, Andrej
Importance of ERK1/2 in Regulation of Protein Translation during Oocyte Meiosis
title Importance of ERK1/2 in Regulation of Protein Translation during Oocyte Meiosis
title_full Importance of ERK1/2 in Regulation of Protein Translation during Oocyte Meiosis
title_fullStr Importance of ERK1/2 in Regulation of Protein Translation during Oocyte Meiosis
title_full_unstemmed Importance of ERK1/2 in Regulation of Protein Translation during Oocyte Meiosis
title_short Importance of ERK1/2 in Regulation of Protein Translation during Oocyte Meiosis
title_sort importance of erk1/2 in regulation of protein translation during oocyte meiosis
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5877559/
https://www.ncbi.nlm.nih.gov/pubmed/29494492
http://dx.doi.org/10.3390/ijms19030698
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