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. 2017 Oct 26;7:14077. doi: 10.1038/s41598-017-13688-3

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Proposed model for the regulation of translation of Cyclins during mouse oocyte maturation. Translation of endogenous Cyclin mRNAs was monitored by measuring ribosome loading onto the mRNAs or exogenously injected reporter accumulation. CPEB1 phosphorylation and reporter translation is independent of Aurora A kinase. It is instead directly or indirectly dependent on Cdk1 activation. Phosphorylated CPEB1 modulates the translation of Ccnb1 whereas Ccnb2 translation is largely independent of CPEB1. The rate of synthesis, rather than that of degradation, of the two proteins is a major determinant of Cyclin levels and of MPF levels in mouse oocytes.