Dissolution of the maskin-eIF4E complex by cytoplasmic polyadenylation and poly(A)-binding protein controls cyclin B1 mRNA translation and oocyte maturation

UMMS Affiliation

Program in Molecular Medicine

Publication Date


Document Type



Adenosine Monophosphate; Animals; Cyclin B; Cytoplasm; Eukaryotic Initiation Factor-4E; Oocytes; Peptide Initiation Factors; Poly(A)-Binding Proteins; RNA, Messenger; RNA-Binding Proteins; Trans-Activation (Genetics)


Life Sciences | Medicine and Health Sciences


Cytoplasmic polyadenylation stimulates the translation of several dormant mRNAs during oocyte maturation in XENOPUS: Polyadenylation is regulated by the cytoplasmic polyadenylation element (CPE), a cis-acting element in the 3'-untranslated region of responding mRNAs, and its associated factor CPEB. CPEB also binds maskin, a protein that in turn interacts with eIF4E, the cap-binding factor. Here, we report that based on antibody and mRNA reporter injection assays, maskin prevents oocyte maturation and the translation of the CPE-containing cyclin B1 mRNA by blocking the association of eIF4G with eIF4E. Dissociation of the maskin-eIF4E complex is essential for cyclin B1 mRNA translational activation, and requires not only cytoplasmic polyadenylation, but also the poly(A)-binding protein. These results suggest a molecular mechanism by which CPE- containing mRNA is activated in early development.

DOI of Published Version



EMBO J. 2002 Jul 15;21(14):3852-62. Link to article on publisher's site

Journal/Book/Conference Title

The EMBO journal

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Link to Article in PubMed

PubMed ID