Aurora Kinase A Is Not Involved in CPEB1 Phosphorylation and cyclin B1 mRNA Polyadenylation during Meiotic Maturation of Porcine Oocytes

0429620 - ÚŽFG 2015 RIV US eng J - Článek v odborném periodiku
Komrsková, Pavla - Šušor, Andrej - Malík, Radek - Procházková, Barbora - Lišková, Lucie - Šupolíková, Jaroslava - Hladký, Štěpán - Kubelka, Michal
Aurora Kinase A Is Not Involved in CPEB1 Phosphorylation and cyclin B1 mRNA Polyadenylation during Meiotic Maturation of Porcine Oocytes.
PLoS ONE. Roč. 9, č. 7 (2014), e101222-e101222. ISSN 1932-6203. E-ISSN 1932-6203
Grant CEP: GA ČR GAP502/10/0944; GA ČR GA13-12291S; GA ČR GAP502/12/2201
Institucionální podpora: RVO:67985904 ; RVO:68378050
Klíčová slova: Aurora Kinase A
Kód oboru RIV: EB - Genetika a molekulární biologie
Impakt faktor: 3.234, rok: 2014
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0101222

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.
Trvalý link: http://hdl.handle.net/11104/0234713