ArticlePloS one2014
Aurora kinase A is not involved in CPEB1 phosphorylation and cyclin B1 mRNA polyadenylation during meiotic maturation of porcine oocytes.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Multiple intersecting pathways are involved in CPEB1 phosphorylation and regulation of translation during mouse oocyte meiosis.Development (Cambridge, England) · 2024Article
- Article
- A genome-wide perspective of the maternal mRNA translation program during oocyte development.Seminars in cell & developmental biology · 2024Review
- Multiple intersecting pathways are involved in the phosphorylation of CPEB1 to activate translation during mouse oocyte meiosis.bioRxiv : the preprint server for biology · 2024Article
- Aurora kinase B inhibits aurora kinase A to control maternal mRNA translation in mouse oocytes.Development (Cambridge, England) · 2021Article
- Translational Control ofCells · 2020Review
- Positive Feedback Stimulation ofFrontiers in cell and developmental biology · 2020Article
- SGK phosphorylates Cdc25 and Myt1 to trigger cyclin B-Cdk1 activation at the meiotic G2/M transition.The Journal of cell biology · 2019Article
- CPEB2 Is Necessary for Proper Porcine Meiotic Maturation and Embryonic Development.International journal of molecular sciences · 2018Article
- Importance of ERK1/2 in Regulation of Protein Translation during Oocyte Meiosis.International journal of molecular sciences · 2018Review
- Article
- The Translation of Cyclin B1 and B2 is Differentially Regulated during Mouse Oocyte Reentry into the Meiotic Cell Cycle.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Regulation of mRNA translation by cytoplasmic polyadenylation is known to be important for oocyte maturation and further development. This process is generally controlled by phosphorylation of cytoplasmic polyadenylation element binding protein 1 (CPEB1). The aim of this study is to determine the role of Aurora kinase A in CPEB1 phosphorylation and the consequent CPEB1-dependent polyadenylation of maternal mRNAs during mammalian oocyte meiosis. For this purpose, we specifically inhibited Aurora kinase A with MLN8237 during meiotic maturation of porcine oocytes. Using poly(A)-test PCR method, we monitored the effect of Aurora kinase A inhibition on poly(A)-tail extension of long and short cyclin B1 encoding mRNAs as markers of CPEB1-dependent cytoplasmic polyadenylation. Our results show that inhibition of Aurora kinase A activity impairs neither cyclin B1 mRNA polyadenylation nor its translation and that Aurora kinase A is unlikely to be involved in CPEB1 activating phosphorylation.
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