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

Quiping Cao1, Joel D Richter

  • 1Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.

The EMBO Journal
|July 12, 2002
PubMed

Insights

Cytoplasmic polyadenylation activates dormant mRNAs for oocyte maturation in Xenopus. This process requires maskin-eIF4E complex dissociation, enabling cyclin B1 mRNA translation.

Area of Science:

  • Molecular Biology
  • Developmental Biology
  • Xenopus Oocyte Maturation

Background:

  • Cytoplasmic polyadenylation is crucial for activating dormant mRNAs during Xenopus oocyte maturation.
  • This process is mediated by the cytoplasmic polyadenylation element (CPE) and its binding factor, CPEB.
  • CPEB interacts with maskin, which then binds to the cap-binding factor eIF4E.

Purpose of the Study:

  • To elucidate the molecular mechanism by which maskin regulates CPE-containing mRNA translation during oocyte maturation.
  • To identify the factors involved in the dissociation of the maskin-eIF4E complex and subsequent mRNA activation.

Main Methods:

  • Antibody injection assays in Xenopus oocytes.
  • mRNA reporter injection assays to study translation.
  • Investigating protein-protein interactions between maskin, eIF4E, and eIF4G.

Main Results:

  • Maskin inhibits oocyte maturation and cyclin B1 mRNA translation by preventing eIF4G from associating with eIF4E.
  • Dissociation of the maskin-eIF4E complex is essential for activating cyclin B1 mRNA translation.
  • This dissociation requires both cytoplasmic polyadenylation and the poly(A)-binding protein.

Conclusions:

  • A molecular mechanism for CPE-containing mRNA activation in early development is proposed.
  • Maskin acts as a translational repressor, and its removal is a key step in oocyte maturation.
  • Cytoplasmic polyadenylation and poly(A)-binding protein are critical for relieving maskin-mediated translational repression.

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