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Gene Review

CPEB1  -  cytoplasmic polyadenylation element...

Homo sapiens

Synonyms: CPE-BP1, CPE-binding protein 1, CPEB, CPEB-1, Cytoplasmic polyadenylation element-binding protein 1, ...
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Disease relevance of CPEB1


High impact information on CPEB1

  • We show that the synthesis of RINGO/Spy, an atypical activator of cyclin-dependent kinases (cdks), is necessary for CPEB-directed polyadenylation [2].
  • CPEB activity requires not only the phosphorylation of S174, but also the synthesis of a heretofore-unknown upstream effector molecule [2].
  • Exogenous CPEB restores senescence in the KO MEFs and also induces precocious senescence in wild-type MEFs [3].
  • These results demonstrate that a reversible Pum2 interaction controls RINGO/Spy mRNA translation and, as a result, CPEB-mediated cytoplasmic polyadenylation [2].
  • Control of cellular senescence by CPEB [3].

Biological context of CPEB1

  • In this study we report the cloning of a human cytoplasmic polyadenylation element binding (hCPEB) protein with sequence-specific RNA binding activity [4].
  • Our data demonstrate that alternative splicing generates hCPEB mRNAs that encode proteins with a conserved C-terminal RNA binding domain but with different N-terminal regulatory domains [4].
  • Here, we demonstrate that the CPE and its binding protein CPEB facilitate mRNA transport to dendrites [5].
  • One target of CPEB regulation is myc mRNA, whose unregulated translation in the KO MEFs may cause them to bypass senescence [3].
  • Regulated Pumilio-2 binding controls RINGO/Spy mRNA translation and CPEB activation [2].

Anatomical context of CPEB1

  • We show that all CPEB1 isoforms are found associated with two previously described cytoplasmic structures, stress granules and dcp1 bodies [6].
  • The hCPEB mRNA is expressed in the brain and heart as well as in immature oocytes, consistent with the hypothesis that cytoplasmic polyadenylation may regulate the translation of human mRNAs in both oocytes and somatic cells [4].
  • In the hippocampus, mouse GLD2 mRNA colocalizes with CPEB1 and Pumilio1 mRNAs, both of which are likely involved in synaptic plasticity [7].
  • To assess the function of CPEB after pachytene, we used the zona pellucida 3 (Zp3) promoter to generate transgenic mice expressing siRNA that induce the destruction of Cpeb mRNA [1].
  • While a CPEB knockout (KO) mouse is sterile but overtly normal, embryo fibroblasts derived from this mouse (MEFs) do not enter senescence in culture as do wild-type MEFs, but instead are immortal [3].

Associations of CPEB1 with chemical compounds

  • To exert this effect, XGef must retain guanine exchange activity and the interaction with CPEB [8].
  • XGef, a guanine exchange factor, is a CPEB-interacting protein involved in the early steps of progesterone-stimulated oocyte maturation [8].
  • In vertebrates, enhanced translation of mRNAs in oocytes and early embryos entering M-phase is thought to occur through polyadenylation, involving binding, hyperphosphorylation and proteolytic degradation of Aurora-activated CPEB [9].

Regulatory relationships of CPEB1


Other interactions of CPEB1


Analytical, diagnostic and therapeutic context of CPEB1


  1. CPEB controls oocyte growth and follicle development in the mouse. Racki, W.J., Richter, J.D. Development (2006) [Pubmed]
  2. Regulated Pumilio-2 binding controls RINGO/Spy mRNA translation and CPEB activation. Padmanabhan, K., Richter, J.D. Genes Dev. (2006) [Pubmed]
  3. Control of cellular senescence by CPEB. Groisman, I., Ivshina, M., Marin, V., Kennedy, N.J., Davis, R.J., Richter, J.D. Genes Dev. (2006) [Pubmed]
  4. Identification and characterization of the gene encoding human cytoplasmic polyadenylation element binding protein. Welk, J.F., Charlesworth, A., Smith, G.D., MacNicol, A.M. Gene (2001) [Pubmed]
  5. Facilitation of dendritic mRNA transport by CPEB. Huang, Y.S., Carson, J.H., Barbarese, E., Richter, J.D. Genes Dev. (2003) [Pubmed]
  6. The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules. Wilczynska, A., Aigueperse, C., Kress, M., Dautry, F., Weil, D. J. Cell. Sci. (2005) [Pubmed]
  7. Vertebrate GLD2 poly(A) polymerases in the germline and the brain. Rouhana, L., Wang, L., Buter, N., Kwak, J.E., Schiltz, C.A., Gonzalez, T., Kelley, A.E., Landry, C.F., Wickens, M. RNA (2005) [Pubmed]
  8. XGef mediates early CPEB phosphorylation during Xenopus oocyte meiotic maturation. Martínez, S.E., Yuan, L., Lacza, C., Ransom, H., Mahon, G.M., Whitehead, I.P., Hake, L.E. Mol. Biol. Cell (2005) [Pubmed]
  9. Nuclear envelope breakdown may deliver an inhibitor of protein phosphatase 1 which triggers cyclin B translation in starfish oocytes. Lapasset, L., Pradet-Balade, B., Lozano, J.C., Peaucellier, G., Picard, A. Dev. Biol. (2005) [Pubmed]
  10. Over-expression of Aurora-A targets cytoplasmic polyadenylation element binding protein and promotes mRNA polyadenylation of Cdk1 and cyclin B1. Sasayama, T., Marumoto, T., Kunitoku, N., Zhang, D., Tamaki, N., Kohmura, E., Saya, H., Hirota, T. Genes Cells (2005) [Pubmed]
  11. CPEB regulation of human cellular senescence, energy metabolism, and p53 mRNA translation. Burns, D.M., Richter, J.D. Genes Dev. (2008) [Pubmed]
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