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.

• MeSH
• Aurora Kinase A metabolism   MeSH
• Cyclin B1 genetics   MeSH
• mRNA Cleavage and Polyadenylation Factors chemistry   metabolism   MeSH
• Phosphorylation MeSH
• Meiosis * MeSH
• RNA, Messenger metabolism   MeSH
• Oocytes enzymology   metabolism   MeSH
• Polyadenylation MeSH
• Sus scrofa metabolism   MeSH
• Animals MeSH
• Check Tag
• Female MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Aurora Kinase A MeSH
• Cyclin B1 MeSH
• mRNA Cleavage and Polyadenylation Factors MeSH
• RNA, Messenger MeSH