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

EMBO J. 2002 Jul 15;21(14):3852-62. doi: 10.1093/emboj/cdf353.

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Monophosphate / metabolism*
  • Animals
  • Cyclin B / genetics*
  • Cyclin B1
  • Cytoplasm / metabolism*
  • Eukaryotic Initiation Factor-4E
  • Oocytes / metabolism*
  • Peptide Initiation Factors / metabolism*
  • Poly(A)-Binding Proteins
  • RNA, Messenger / genetics*
  • RNA-Binding Proteins / metabolism*
  • Transcriptional Activation

Substances

  • Cyclin B
  • Cyclin B1
  • Eukaryotic Initiation Factor-4E
  • Peptide Initiation Factors
  • Poly(A)-Binding Proteins
  • RNA, Messenger
  • RNA-Binding Proteins
  • Adenosine Monophosphate