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B, and Stress-Activated Protein Kinase1
*
Departments of Microbiology and Molecular Genetics and Medicine, Harvard Medical School and Brigham and Women’s Hospital, Boston, MA 02115; and
Department of Microbiology and Immunology, Lineberger Comprehensive Cancer Center, University of North Carolina School of Medicine, Chapel Hill, NC 27599
The EBV latent infection transforming protein, LMP1, has six
hydrophobic transmembrane domains that enable it to aggregate in the
plasma membrane and a 200-amino acid carboxyl-terminal cytoplasmic
domain (CT) that activates nuclear factor-
B and induces many of the
phenotypic changes in B lymphocytes that accompany CD40 activation.
Since the phenotypic effects of LMP1 are similar to those of activated
CD40, we now compare signaling from the LMP1 CT with that from the CD40
CT fused to the LMP1 transmembrane domains. The LMPCD40 chimera was
similar to LMP1 in nuclear factor-B activation and in up-regulation
of epidermal growth factor receptor expression. CD40 ligation was known
to activate the stress-activated protein kinase, and both LMPCD40 and
LMP1 are now shown to induce stress-activated protein kinase activity
in the absence of ligand. Deletion of the first four transmembrane
domains of LMP1 abrogated LMP1 aggregation in the plasma membrane and
nearly abolished signaling from LMP1 or the LMPCD40 chimera. These
results highlight the role of LMP1 as a constitutively active receptor
similar to CD40 and provide a novel approach for the generation of
ligand-independent receptors.
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O. Devergne, E. C. McFarland, G. Mosialos, K. M. Izumi, C. F. Ware, and E. Kieff Role of the TRAF Binding Site and NF-kappa B Activation in Epstein-Barr Virus Latent Membrane Protein 1-Induced Cell Gene Expression J. Virol., October 1, 1998; 72(10): 7900 - 7908. [Abstract] [Full Text] [PDF]
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B. S. Sylla, S. C. Hung, D. M. Davidson, E. Hatzivassiliou, N. L. Malinin, D. Wallach, T. D. Gilmore, E. Kieff, and G. Mosialos Epstein-Barr virus-transforming protein latent infection membrane protein 1 activates transcription factor NF-kappa B through a pathway that includes the NF-kappa B-inducing kinase and the Ikappa B kinases IKKalpha and IKKbeta PNAS, August 18, 1998; 95(17): 10106 - 10111. [Abstract] [Full Text] [PDF]
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A. C. Grammer, J. L. Swantek, R. D. McFarland, Y. Miura, T. Geppert, and P. E. Lipsky TNF Receptor-Associated Factor-3 Signaling Mediates Activation of p38 and Jun N-Terminal Kinase, Cytokine Secretion, and Ig Production Following Ligation of CD40 on Human B Cells J. Immunol., August 1, 1998; 161(3): 1183 - 1193. [Abstract] [Full Text] [PDF]
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W. E. Miller, J. L. Cheshire, and N. Raab-Traub Interaction of Tumor Necrosis Factor Receptor-Associated Factor Signaling Proteins with the Latent Membrane Protein 1 PXQXT Motif Is Essential for Induction of Epidermal Growth Factor Receptor Expression Mol. Cell. Biol., May 1, 1998; 18(5): 2835 - 2844. [Abstract] [Full Text]
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M. A. Luftig, E. Cahir-McFarland, G. Mosialos, and E. Kieff Effects of the NIK aly Mutation on NF-kappa B Activation by the Epstein-Barr Virus Latent Infection Membrane Protein, Lymphotoxin beta Receptor, and CD40 J. Biol. Chem., April 27, 2001; 276(18): 14602 - 14606. [Abstract] [Full Text] [PDF]
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E. D. Cahir-McFarland, D. M. Davidson, S. L. Schauer, J. Duong, and E. Kieff NF-kappa B inhibition causes spontaneous apoptosis in Epstein-Barr virus-transformed lymphoblastoid cells PNAS, May 23, 2000; 97(11): 6055 - 6060. [Abstract] [Full Text] [PDF]
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