Title

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

7-12-2002

Document Type

Article

Subjects

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)

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

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.

Rights and Permissions

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

DOI of Published Version

10.1093/emboj/cdf353

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

The EMBO journal

PubMed ID

12110596