Phosphorylation of CPE binding factor by Eg2 regulates translation of c-mos mRNA

Raul Mendez, Laura E. Hake, Thorkell Andresson, Laurie E. Littlepage, Joan V. Ruderman and Joel D. Richter ()
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Raul Mendez: University of Massachusetts Medical Center
Laura E. Hake: University of Massachusetts Medical Center
Thorkell Andresson: Harvard Medical School
Laurie E. Littlepage: Harvard Medical School
Joan V. Ruderman: Harvard Medical School
Joel D. Richter: University of Massachusetts Medical Center

Nature, 2000, vol. 404, issue 6775, 302-307

Abstract: Abstract Full-grown Xenopus oocytes arrest at the G2/M border of meiosis I. Progesterone breaks this arrest, leading to the resumption of the meiotic cell cycles and maturation of the oocyte into a fertilizable egg. In these oocytes, progesterone interacts with an unidentified surface-associated receptor, which induces a non-transcriptional signalling pathway that stimulates the translation of dormant c-mos messenger RNA. Mos, a mitogen-activated protein (MAP) kinase kinase kinase, indirectly activates MAP kinase, which in turn leads to oocyte maturation. The translational recruitment of c- mos and several other mRNAs is regulated by cytoplasmic polyadenylation, a process that requires two 3′ untranslated regions, the cytoplasmic polyadenylation element (CPE) and the polyadenylation hexanucleotide AAUAAA1,2,3,4. Although the signalling events that trigger c-mos mRNA polyadenylation and translation are unclear, they probably involve the activation of CPEB, the CPE binding factor5,6. Here we show that an early site-specific phosphorylation of CPEB is essential for the polyadenylation of c-mos mRNA and its subsequent translation, and for oocyte maturation. In addition, we show that this selective, early phosphorylation of CPEB is catalysed by Eg2, a member of the Aurora family of serine/threonine protein kinases.

Date: 2000
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DOI: 10.1038/35005126

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