| First Author | Stebbins-Boaz B | Year | 1999 |
| Journal | Mol Cell | Volume | 4 |
| Issue | 6 | Pages | 1017-27 |
| PubMed ID | 10635326 | Mgi Jnum | J:59157 |
| Mgi Id | MGI:1351096 | Doi | 10.1016/s1097-2765(00)80230-0 |
| Citation | Stebbins-Boaz B, et al. (1999) Maskin is a CPEB-associated factor that transiently interacts with elF-4E. Mol Cell 4(6):1017-27 |
| abstractText | 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. |
