Maskin is a CPEB-associated factor that transiently interacts with eIF-4E

被引：306

作者：

Stebbins-Boaz, B ^{[1
]}

Cao, QP ^{[1
]}

de Moor, CH ^{[1
]}

Mendez, R ^{[1
]}

Richter, JD ^{[1
]}

机构：

[1] Univ Massachusetts, Sch Med, Dept Mol Genet & Microbiol, Worcester, MA 01655 USA

来源：

MOLECULAR CELL | 1999年 / 4卷 / 06期

关键词：

D O I：

10.1016/S1097-2765(00)80230-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In Xenopus, the CPE is a bifunctional 3' UTR sequence that maintains maternal mRNA in a dormant state in oocytes and activates polyadenylation-induced translation during oocyte maturation. Here, we report that CPEB, which binds the CPE and stimulates polyadenylation, interacts with a new factor we term maskin. Maskin contains a peptide sequence that is conserved among elF-4E-binding proteins. Affinity chromatography demonstrates that CPEB, maskin, and elF-4E reside in a complex in oocytes, and yeast two-hybrid analyses indicate that CPEB and maskin bind directly, as do maskin and elF-4E. While CPEB and maskin remain together during oocyte maturation, the maskin-elF-4E interaction is substantially reduced. The dissolution of this complex may result in the binding of elF-4E to elF-4G and the translational activation of CPE-containing mRNAs.

引用

页码：1017 / 1027

页数：11

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