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 Everly, D. N.
Right arrow Articles by Raab-Traub, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Everly, D. N., Jr.
Right arrow Articles by Raab-Traub, N.

 Previous Article  |  Next Article 

Journal of Virology, November 2004, p. 11648-11655, Vol. 78, No. 21
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.21.11648-11655.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Accumulation of Cytoplasmic ß-Catenin and Nuclear Glycogen Synthase Kinase 3ß in Epstein-Barr Virus-Infected Cells

David N. Everly Jr.,1 Shuichi Kusano,1,2 and Nancy Raab-Traub1*

Lineberger Comprehensive Cancer Center, School of Medicine, University of North Carolina, Chapel Hill, North Carolina,1 Department of Microbiology, St. Marianna University School of Medicine, Kawasaki, Kanagawa, Japan2

Received 4 May 2004/ Accepted 21 June 2004

Epstein-Barr virus (EBV) causes infectious mononucleosis and is associated with cancers in immunocompromised populations. EBV establishes a latent infection and immortalizes and transforms B lymphocytes. Several latent proteins have profound effects on cellular growth, including activation of NF-{kappa}B, phosphatidylinositol 3'-OH kinase (PI3K) signaling, and notch signaling. Activation of PI3K can affect the activity of ß-catenin, the target of the wnt signaling pathway. Deregulation of ß-catenin is associated with a number of malignancies. To determine if ß-catenin is regulated by EBV infection, EBV-infected cells were examined for ß-catenin levels and localization. ß-Catenin was increased in EBV-positive tumor cell lines compared to EBV-negative lines, in EBV-infected Burkitt's lymphoma cell lines, and in EBV-transformed lymphoblastoid cell lines (LCL). In contrast to wnt signaling, EBV consistently induced the accumulation of ß-catenin in the cytoplasm but not the nucleus. The ß-catenin regulating kinase, glycogen synthase kinase 3ß (GSK3ß), was shown to be phosphorylated and inactivated in EBV-infected lymphocytes. Inactivated GSK3ß was localized to the nucleus of EBV-infected LCL. Neither the cytoplasmic accumulation of ß-catenin nor the nuclear inactivation of GSK3ß was affected by the inhibition of PI3K signaling. These data indicate that latent infection with EBV has unique effects on ß-catenin signaling that are distinct from activation of wnt and independent of its effects on PI3K.

* Corresponding author. Mailing address: Lineberger Comprehensive Cancer Center, University of North Carolina—Chapel Hill, Mason Farm Rd., Room 102, Chapel Hill, NC 27599. Phone: (919) 966-1701. Fax: (919) 966-9673. E-mail: nrt{at}med.unc.edu.

Journal of Virology, November 2004, p. 11648-11655, Vol. 78, No. 21
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.21.11648-11655.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Shair, K. H.Y, Schnegg, C. I., Raab-Traub, N. (2009). Epstein-Barr Virus Latent Membrane Protein-1 Effects on Junctional Plakoglobin and Induction of a Cadherin Switch. Cancer Res. 69: 5734-5742 [Abstract] [Full Text]  
  • Shair, K. H.Y., Schnegg, C. I., Raab-Traub, N. (2008). EBV Latent Membrane Protein 1 Effects on Plakoglobin, Cell Growth, and Migration. Cancer Res. 68: 6997-7005 [Abstract] [Full Text]  
  • Jung, J. K., Kwun, H. J., Lee, J.-O., Arora, P., Jang, K. L. (2007). Hepatitis B virus X protein differentially affects the ubiquitin-mediated proteasomal degradation of beta-catenin depending on the status of cellular p53. J. Gen. Virol. 88: 2144-2154 [Abstract] [Full Text]  
  • Mainou, B. A., Raab-Traub, N. (2006). LMP1 Strain Variants: Biological and Molecular Properties.. J. Virol. 80: 6458-6468 [Abstract] [Full Text]  
  • Hayward, S. D., Liu, J., Fujimuro, M. (2006). Notch and Wnt Signaling: Mimicry and Manipulation by Gamma Herpesviruses. Sci Signal 2006: re4-re4 [Abstract] [Full Text]  
  • Jang, K. L., Shackelford, J., Seo, S. Y., Pagano, J. S. (2005). Up-regulation of {beta}-catenin by a viral oncogene correlates with inhibition of the seven in absentia homolog 1 in B lymphoma cells. Proc. Natl. Acad. Sci. USA 102: 18431-18436 [Abstract] [Full Text]  
  • Fujimuro, M., Liu, J., Zhu, J., Yokosawa, H., Hayward, S. D. (2005). Regulation of the Interaction between Glycogen Synthase Kinase 3 and the Kaposi's Sarcoma-Associated Herpesvirus Latency-Associated Nuclear Antigen. J. Virol. 79: 10429-10441 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»