Previous Article | Next Article 
Journal of Virology, January 2002, p. 455-459, Vol. 76, No. 1
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.76.1.455-459.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
The Epstein-Barr Virus Latent Membrane Protein 1 Putative Janus Kinase 3 (JAK3) Binding Domain Does Not Mediate JAK3 Association or Activation in B-Lymphoma or Lymphoblastoid Cell Lines
Masaya Higuchi,
, Elliott Kieff, and Kenneth M. Izumi*
Channing Laboratory and Department of Medicine, Brigham and Womens Hospital, and Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115-5804
Received 24 July 2001/
Accepted 25 September 2001
Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1) has an intermediate domain between the two cytoplasmic carboxyl-terminal domains that are critical for transforming B-lymphocytes into lymphoblastoid cell lines (LCLs). The intermediate domain has been implicated in Janus kinase 3 (JAK3) association and activation. We now find that LCLs transformed by EBV recombinants that express Flag-LMP1 with the putative JAK3 binding and activating intermediate domain deleted and LCLs transformed by Flag-LMP1 EBV recombinants have similar levels of phosphotyrosine-activated JAK3, signal transducer and activator of transcription 3 (STAT3), or STAT5 and similar very low levels of JAK3 associated with LMP1. Further, transient Flag-LMP1 expression in a B-lymphoma cell line transduces signals that upregulate TRAF1 levels but does not alter JAK3 levels or activation state. Although these data indicate that the LMP1 putative JAK3 binding and activating intermediate domain does not mediate JAK3 association or activation in B-lymphocytes, JAK3 association with LMP1 could be significant, particularly in cells in which LMP1, JAK3, or a JAK3-associated protein is expressed at high levels.
* Corresponding author. Present address: University of Texas Health Science Center, Department of Microbiology, 7703 Floyd Curl Dr., San Antonio, TX 78229-3900. Phone: (210) 567-3935. Fax: (210) 567-6412. E-mail: izumi{at}uthscsa.edu.
Present address: Niigata University School of Medicine, Dept. of Virology, Niigata, Japan 951-8510.
Journal of Virology, January 2002, p. 455-459, Vol. 76, No. 1
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.76.1.455-459.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
This article has been cited by other articles:
-
Kung, C.-P., Raab-Traub, N.
(2008). Epstein-Barr Virus Latent Membrane Protein 1 Induces Expression of the Epidermal Growth Factor Receptor through Effects on Bcl-3 and STAT3. J. Virol.
82: 5486-5493
[Abstract]
[Full Text]
-
Mainou, B. A., Everly, D. N. Jr., Raab-Traub, N.
(2007). Unique Signaling Properties of CTAR1 in LMP1-Mediated Transformation. J. Virol.
81: 9680-9692
[Abstract]
[Full Text]
-
Pandya, J., Walling, D. M.
(2006). Oncogenic Activity of Epstein-Barr Virus Latent Membrane Protein 1 (LMP-1) Is Down-Regulated by Lytic LMP-1.. J. Virol.
80: 8038-8046
[Abstract]
[Full Text]
-
Brinkmann, M. M., Schulz, T. F.
(2006). Regulation of intracellular signalling by the terminal membrane proteins of members of the Gammaherpesvirinae.. J. Gen. Virol.
87: 1047-1074
[Abstract]
[Full Text]
-
Xu, D., Brumm, K., Zhang, L.
(2006). The Latent Membrane Protein 1 of Epstein-Barr Virus (EBV) Primes EBV Latency Cells for Type I Interferon Production. J. Biol. Chem.
281: 9163-9169
[Abstract]
[Full Text]
-
Le Clorennec, C., Youlyouz-Marfak, I., Adriaenssens, E., Coll, J., Bornkamm, G. W., Feuillard, J.
(2006). EBV latency III immortalization program sensitizes B cells to induction of CD95-mediated apoptosis via LMP1: role of NF-{kappa}B, STAT1, and p53. Blood
107: 2070-2078
[Abstract]
[Full Text]
-
Najjar, I., Baran-Marszak, F., Le Clorennec, C., Laguillier, C., Schischmanoff, O., Youlyouz-Marfak, I., Schlee, M., Bornkamm, G. W., Raphael, M., Feuillard, J., Fagard, R.
(2005). Latent Membrane Protein 1 Regulates STAT1 through NF-{kappa}B-Dependent Interferon Secretion in Epstein-Barr Virus-Immortalized B Cells. J. Virol.
79: 4936-4943
[Abstract]
[Full Text]
-
Pandya, J., Walling, D. M.
(2004). Epstein-Barr Virus Latent Membrane Protein 1 (LMP-1) Half-Life in Epithelial Cells Is Down-Regulated by Lytic LMP-1. J. Virol.
78: 8404-8410
[Abstract]
[Full Text]
-
Yasui, T., Luftig, M., Soni, V., Kieff, E.
(2004). Latent infection membrane protein transmembrane FWLY is critical for intermolecular interaction, raft localization, and signaling. Proc. Natl. Acad. Sci. USA
101: 278-283
[Abstract]
[Full Text]
-
Dirmeier, U., Neuhierl, B., Kilger, E., Reisbach, G., Sandberg, M. L., Hammerschmidt, W.
(2003). Latent Membrane Protein 1 Is Critical for Efficient Growth Transformation of Human B Cells by Epstein-Barr Virus. Cancer Res.
63: 2982-2989
[Abstract]
[Full Text]
-
Chen, H., Hutt-Fletcher, L., Cao, L., Hayward, S. D.
(2003). A Positive Autoregulatory Loop of LMP1 Expression and STAT Activation in Epithelial Cells Latently Infected with Epstein-Barr Virus. J. Virol.
77: 4139-4148
[Abstract]
[Full Text]
-
Aoki, Y., Feldman, G. M., Tosato, G.
(2003). Inhibition of STAT3 signaling induces apoptosis and decreases survivin expression in primary effusion lymphoma. Blood
101: 1535-1542
[Abstract]
[Full Text]
-
Eliopoulos, A. G., Waites, E. R., Blake, S. M. S., Davies, C., Murray, P., Young, L. S.
(2002). TRAF1 Is a Critical Regulator of JNK Signaling by the TRAF-Binding Domain of the Epstein-Barr Virus-Encoded Latent Infection Membrane Protein 1 but Not CD40. J. Virol.
77: 1316-1328
[Abstract]
[Full Text]
Copyright © 2002 by the American Society for Microbiology. All rights reserved.