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

Mol Cell. 1999 Dec;4(6):1017-27. doi: 10.1016/s1097-2765(00)80230-0.

Abstract

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.

Publication types

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

MeSH terms

  • 3' Untranslated Regions / genetics
  • Amino Acid Sequence
  • Animals
  • Eukaryotic Initiation Factor-4E
  • Female
  • Molecular Sequence Data
  • Oocytes
  • Peptide Initiation Factors / genetics*
  • Protein Biosynthesis*
  • RNA-Binding Proteins / genetics*
  • Sequence Alignment
  • Transcription Factors / genetics*
  • Xenopus / genetics*
  • Xenopus Proteins*
  • mRNA Cleavage and Polyadenylation Factors*

Substances

  • 3' Untranslated Regions
  • Cpeb1 protein, Xenopus
  • Eukaryotic Initiation Factor-4E
  • Peptide Initiation Factors
  • RNA-Binding Proteins
  • Transcription Factors
  • Xenopus Proteins
  • mRNA Cleavage and Polyadenylation Factors

Associated data

  • GENBANK/AF200212