This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jung, M.-Y.
Right arrow Articles by Richter, J. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jung, M.-Y.
Right arrow Articles by Richter, J. D.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, June 2006, p. 4277-4287, Vol. 26, No. 11
0270-7306/06/$08.00+0     doi:10.1128/MCB.02470-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Translational Control by Neuroguidin, a Eukaryotic Initiation Factor 4E and CPEB Binding Protein

Mi-Young Jung, Lori Lorenz, and Joel D. Richter*

Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605

Received 27 December 2005/ Returned for modification 8 February 2006/ Accepted 8 March 2006

CPEB-mediated translation is important in early development and neuronal synaptic plasticity. Here, we describe a new eukaryotic initiation factor 4E (eIF4E) binding protein, Neuroguidin (Ngd), and its interaction with CPEB. In the mammalian nervous system, Ngd is detected as puncta in axons and dendrites and in growth cones and filopodia. Ngd contains three motifs that resemble those present in eIF4G, 4EBP, Cup, and Maskin, all of which are eIF4E binding proteins. Ngd binds eIF4E directly, and all three motifs must be deleted to abrogate the interaction between these two proteins. In injected Xenopus oocytes, Ngd binds CPEB and, most importantly, represses translation in a cytoplasmic polyadenylation element (CPE)-dependent manner. In Xenopus embryos, Ngd is found in both neural tube and neural crest cells. The injection of morpholino-containing antisense oligonucleotides directed against ngd mRNA disrupts neural tube closure and neural crest migration; however, the wild-type phenotype is restored by the injection of a rescuing ngd mRNA. These data suggest that Ngd guides neural development by regulating the translation of CPE-containing mRNAs.


* Corresponding author. Mailing address: Program in Molecular Medicine, University of Massachusetts Medical School, Suite 204, 373 Plantation St., Worcester MA 01605. Phone: (508) 856-8615. Fax: (508) 856-4289. E-mail: Joel.Richter{at}umassmed.edu.


Molecular and Cellular Biology, June 2006, p. 4277-4287, Vol. 26, No. 11
0270-7306/06/$08.00+0     doi:10.1128/MCB.02470-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Rhoads, R. E. (2009). eIF4E: New Family Members, New Binding Partners, New Roles. J. Biol. Chem. 284: 16711-16715 [Abstract] [Full Text]  
  • Richter, J. D., Klann, E. (2009). Making synaptic plasticity and memory last: mechanisms of translational regulation. Genes Dev. 23: 1-11 [Abstract] [Full Text]  
  • Sihn, C.-R., Lee, Y.-S., Jeong, J.-S., Park, K., Kim, S. H. (2008). CANu1, a novel nucleolar protein, accumulated on centromere in response to DNA damage. GENES CELLS 13: 787-796 [Abstract] [Full Text]  
  • Groisman, I., Ivshina, M., Marin, V., Kennedy, N. J., Davis, R. J., Richter, J. D. (2006). Control of cellular senescence by CPEB. Genes Dev. 20: 2701-2712 [Abstract] [Full Text]