Translational control by cytoplasmic polyadenylation in Xenopus oocytes

Biochim Biophys Acta. 2008 Apr;1779(4):217-29. doi: 10.1016/j.bbagrm.2008.02.002. Epub 2008 Feb 14.

Abstract

Elongation of the poly(A) tails of specific mRNAs in the cytoplasm is a crucial regulatory step in oogenesis and early development of many animal species. The best studied example is the regulation of translation by cytoplasmic polyadenylation elements (CPEs) in the 3' untranslated region of mRNAs involved in Xenopus oocyte maturation. In this review we discuss the mechanism of translational control by the CPE binding protein (CPEB) in Xenopus oocytes as follows: 1. The cytoplasmic polyadenylation machinery such as CPEB, the subunits of cleavage and polyadenylation specificity factor (CPSF), symplekin, Gld-2 and poly(A) polymerase (PAP). 2. The signal transduction that leads to the activation of CPE-mediated polyadenylation during oocyte maturation, including the potential roles of kinases such as MAPK, Aurora A, CamKII, cdk1/Ringo and cdk1/cyclin B. 3. The role of deadenylation and translational repression, including the potential involvement of PARN, CCR4/NOT, maskin, pumilio, Xp54 (Ddx6, Rck), other P-body components and isoforms of the cap binding initiation factor eIF4E. Finally we discuss some of the remaining questions regarding the mechanisms of translational regulation by cytoplasmic polyadenylation and give our view on where our knowledge is likely to be expanded in the near future.

Publication types

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

MeSH terms

  • Animals
  • Cytoplasm / metabolism*
  • Female
  • Oocytes / cytology
  • Oocytes / metabolism*
  • Oogenesis / physiology
  • Poly A / metabolism*
  • Polyadenylation / physiology*
  • Polynucleotide Adenylyltransferase / metabolism*
  • Protein Biosynthesis / physiology*
  • Protein Kinases / metabolism
  • RNA-Binding Proteins / metabolism*
  • Signal Transduction / physiology
  • Xenopus
  • Xenopus Proteins / metabolism*

Substances

  • RNA-Binding Proteins
  • Xenopus Proteins
  • Poly A
  • Protein Kinases
  • Polynucleotide Adenylyltransferase