Nejvíce citovaný článek - PubMed ID 10635326
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 kinasa A metabolismus MeSH
- cyklin B1 genetika MeSH
- faktory štěpení a polyadenylace mRNA chemie metabolismus MeSH
- fosforylace MeSH
- meióza * MeSH
- messenger RNA metabolismus MeSH
- oocyty enzymologie metabolismus MeSH
- polyadenylace MeSH
- Sus scrofa metabolismus MeSH
- zvířata MeSH
- Check Tag
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aurora kinasa A MeSH
- cyklin B1 MeSH
- faktory štěpení a polyadenylace mRNA MeSH
- messenger RNA MeSH