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, Joel D. Richter

Research output: Contribution to journalArticlepeer-review

301 Scopus citations


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 AAUAAA. Although the signalling events that trigger c-mos mRNA polyadenylation and translation are unclear, they probably involve the activation of CPEB, the CPE binding factor. 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.

Original languageEnglish (US)
Pages (from-to)302-307
Number of pages6
Issue number6775
StatePublished - Mar 16 2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General


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