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Maskin is a CPEB-associated factor that transiently interacts with elF-4E
B Stebbins-Boaz1, Q Cao, C H de Moor
1Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester 01655, USA.
Molecular Cell
|January 15, 2000
Summary
Researchers discovered maskin, a protein that interacts with CPEB and eukaryotic initiation factor 4E (eIF-4E) to regulate mRNA translation during Xenopus oocyte maturation.
Area of Science:
- Molecular Biology
- Developmental Biology
- Xenopus laevis research
Background:
- The cytoplasmic polyadenylation element (CPE) in Xenopus 3' UTRs controls mRNA dormancy in oocytes and translation during maturation.
- CPEB (CPE-binding protein) binds CPE and promotes polyadenylation-induced translation.
Purpose of the Study:
- To identify novel factors involved in regulating CPE-mediated translational control.
- To elucidate the molecular mechanism of translational activation during oocyte maturation.
Main Methods:
- Affinity chromatography to identify protein complexes.
- Yeast two-hybrid assays to confirm direct protein interactions.
Main Results:
- A new protein, maskin, was identified that binds both CPEB and eukaryotic initiation factor 4E (eIF-4E).
- CPEB, maskin, and eIF-4E form a complex in oocytes.
- The maskin-eIF-4E interaction diminishes during oocyte maturation, potentially releasing eIF-4E for translation initiation.
Conclusions:
- Maskin acts as a bridge between CPEB and eIF-4E, mediating translational repression in oocytes.
- Dissociation of maskin from eIF-4E is a key step in activating translation of maternal mRNAs during Xenopus oocyte maturation.