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 Matskova, L.
Right arrow Articles by Winberg, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Matskova, L.
Right arrow Articles by Winberg, G.

 Previous Article  |  Next Article 

Journal of Virology, November 2001, p. 10941-10949, Vol. 75, No. 22
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.22.10941-10949.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

C-Terminal Domain of the Epstein-Barr Virus LMP2A Membrane Protein Contains a Clustering Signal

Liudmila Matskova,1 Ingemar Ernberg,1 Tony Pawson,2 and Gösta Winberg1,3,*

Karolinska Institutet, Microbiology and Tumor Biology Center (MTC), SE-171 77 Stockholm,1 Swedish Institute for Infectious Disease Control, Department of Virology, SE-171 82 Solna,3 Sweden, and Samuel Lunefeld Research Institute, Mount Sinai Hospital, Toronto M5G 1X5, Canada2

Received 14 June 2001/Accepted 17 August 2001

The latency-regulated transmembrane protein LMP2A interferes with signaling from the B-cell antigen receptor by recruiting the tyrosine kinases Lyn and Syk and by targeting them for degradation by binding the cellular E3 ubiquitin ligase AIP4. It has been hypothesized that this constitutive activity of LMP2A requires clustering in the membrane, but molecular evidence for this has been lacking. In the present study we show that LMP2A coclusters with chimeric rat CD2 transmembrane molecules carrying the 27-amino-acid (aa) intracellular C terminus of LMP2A and that this C-terminal domain fused to the glutathione-S-transferase protein associates with LMP2A in cell lysates. This molecular association requires neither the cysteine-rich region between aa 471 and 480 nor the terminal three aa 495 to 497. We also show that the juxtamembrane cysteine repeats in the LMP2A C terminus are the major targets for palmitoylation but that this acylation is not required for targeting of LMP2A to detergent-insoluble glycolipid-enriched membrane microdomains.


* Corresponding author. Mailing address: Karolinska Institutet, MTC, P.O. Box 280, SE-171 77 Stockholm, Sweden. Phone: 468 457 2610; 468 728 6749. Fax: 468 31 9470. E-mail: Gosta.Winberg{at}mtc.ki.se.


Journal of Virology, November 2001, p. 10941-10949, Vol. 75, No. 22
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.22.10941-10949.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Rechsteiner, M. P., Berger, C., Zauner, L., Sigrist, J. A., Weber, M., Longnecker, R., Bernasconi, M., Nadal, D. (2008). Latent Membrane Protein 2B Regulates Susceptibility to Induction of Lytic Epstein-Barr Virus Infection. J. Virol. 82: 1739-1747 [Abstract] [Full Text]  
  • Rechsteiner, M. P., Berger, C., Weber, M., Sigrist, J. A., Nadal, D., Bernasconi, M. (2007). Silencing of latent membrane protein 2B reduces susceptibility to activation of lytic Epstein-Barr virus in Burkitt's lymphoma Akata cells. J. Gen. Virol. 88: 1454-1459 [Abstract] [Full Text]  
  • Rovedo, M., Longnecker, R. (2007). Epstein-Barr Virus Latent Membrane Protein 2B (LMP2B) Modulates LMP2A Activity. J. Virol. 81: 84-94 [Abstract] [Full Text]  
  • Ingham, R. J., Raaijmakers, J., Lim, C. S. H., Mbamalu, G., Gish, G., Chen, F., Matskova, L., Ernberg, I., Winberg, G., Pawson, T. (2005). The Epstein-Barr Virus Protein, Latent Membrane Protein 2A, Co-opts Tyrosine Kinases Used by the T Cell Receptor. J. Biol. Chem. 280: 34133-34142 [Abstract] [Full Text]  
  • Allen, M. D., Young, L. S., Dawson, C. W. (2005). The Epstein-Barr Virus-Encoded LMP2A and LMP2B Proteins Promote Epithelial Cell Spreading and Motility. J. Virol. 79: 1789-1802 [Abstract] [Full Text]  
  • Katzman, R. B., Longnecker, R. (2004). LMP2A Does Not Require Palmitoylation To Localize to Buoyant Complexes or for Function. J. Virol. 78: 10878-10887 [Abstract] [Full Text]