The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family
The cytoplasmic C-terminus of Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1) is essential for B lymphocyte growth transformation and is now shown to interact with a novel human protein (LMP1-associated protein 1 [LAP1]). LAN is homologous to a murine protein, tumor necrosis fact...
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| Published in | Cell Vol. 80; no. 3; pp. 389 - 399 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
10.02.1995
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| Subjects | |
| Online Access | Get full text |
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| Abstract | The cytoplasmic C-terminus of Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1) is essential for B lymphocyte growth transformation and is now shown to interact with a novel human protein (LMP1-associated protein 1 [LAP1]). LAN is homologous to a murine protein, tumor necrosis factor receptor-associated factor 2 (TRAF2), implicated in growth signaling from the p80 TNFR. A second novel protein (EBI6), induced by EBV infection, is the human homolog of a second murine TNFR-associated protein (TRAF1). LMP1 expression causes LAPP and EBI6 to localize to LMP1 clusters in lymphoblast plasma membranes, and LMPI coimmunoprecipitates with these proteins. LAPI binds to the p80 TNFR, CD40, and the lymphotoxin-β receptor, while EBI6 associates with the p80 TNFR. The interaction of LMP1 with these TNFR family-associated proteins is further evidence for their role in signaling and links LMP1-mediated transformation to signal transduction from the TNFR family. |
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| AbstractList | The cytoplasmic C-terminus of Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1) is essential for B lymphocyte growth transformation and is now shown to interact with a novel human protein (LMP1-associated protein 1 [LAP1]). LAP1 is homologous to a murine protein, tumor necrosis factor receptor-associated factor 2 (TRAF2), implicated in growth signaling from the p80 TNFR. A second novel protein (EBI6), induced by EBV infection, is the human homolog of a second murine TNFR-associated protein (TRAF1). LMP1 expression causes LAP1 and EBI6 to localize to LMP1 clusters in lymphoblast plasma membranes, and LMP1 coimmunoprecipitates with these proteins. LAP1 binds to the p80 TNFR, CD40, and the lymphotoxin-beta receptor, while EBI6 associates with the p80 TNFR. The interaction of LMP1 with these TNFR family-associated proteins is further evidence for their role in signaling and links LMP1-mediated transformation to signal transduction from the TNFR family. The cytoplasmic C-terminus of Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1) is essential for B lymphocyte growth transformation and is now shown to interact with a novel human protein (LMP1-associated protein 1 [LAP1]). LAP1 is homologous to a murine protein, tumor necrosis factor receptor-associated factor 2 (TRAF2), implicated in growth signalling from the p80 TNFR. A second novel protein (EBI6), induced by EBV infection, is the human homolog of a second murine TNFR-associated protein (TRAF1). LMP1 expression causes LAP1 and EBI6 to localize to LMP1 clusters in lymphoblast plasma membranes, and LMP1 coimmunoprecipitates with these proteins. LAP1 binds to the p80 TNFR, CD40, and the lympho-toxin- beta receptor, while EBI6 associates with the p80 TNFR. The interaction of LMP1 with these TNFR family-associated proteins is further evidence for their role in signaling and links LMP1-mediated transformation to signal transduction from the TNFR family. The cytoplasmic C-terminus of Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1) is essential for B lymphocyte growth transformation and is now shown to interact with a novel human protein (LMP1-associated protein 1 [LAP1]). LAN is homologous to a murine protein, tumor necrosis factor receptor-associated factor 2 (TRAF2), implicated in growth signaling from the p80 TNFR. A second novel protein (EBI6), induced by EBV infection, is the human homolog of a second murine TNFR-associated protein (TRAF1). LMP1 expression causes LAPP and EBI6 to localize to LMP1 clusters in lymphoblast plasma membranes, and LMPI coimmunoprecipitates with these proteins. LAPI binds to the p80 TNFR, CD40, and the lymphotoxin-β receptor, while EBI6 associates with the p80 TNFR. The interaction of LMP1 with these TNFR family-associated proteins is further evidence for their role in signaling and links LMP1-mediated transformation to signal transduction from the TNFR family. |
| Author | Mosialos, George Kleff, Elliott Yalamanchill, Ramana Birkenbacht, Mark Van Arsdale, Todd Ware, Carl |
| Author_xml | – sequence: 1 givenname: George surname: Mosialos fullname: Mosialos, George organization: Department of Medicine Department of Microbiology and Molecular Genetics Harvard Medical School Boston, Massachusetts 02115 USA – sequence: 2 givenname: Mark surname: Birkenbacht fullname: Birkenbacht, Mark organization: Department of Pathology Marjorie B. Kovler Viral Oncology Laboratories University of Chicago Chicago, Illinois 60637 USA – sequence: 3 givenname: Ramana surname: Yalamanchill fullname: Yalamanchill, Ramana organization: Department of Medicine Department of Microbiology and Molecular Genetics Harvard Medical School Boston, Massachusetts 02115 USA – sequence: 4 givenname: Todd surname: Van Arsdale fullname: Van Arsdale, Todd organization: Division of Biomedical Sciences University of California Riverside, California 92521 USA – sequence: 5 givenname: Carl surname: Ware fullname: Ware, Carl organization: Department of Medicine Department of Microbiology and Molecular Genetics Harvard Medical School Boston, Massachusetts 02115 USA – sequence: 6 givenname: Elliott surname: Kleff fullname: Kleff, Elliott organization: Department of Medicine Department of Microbiology and Molecular Genetics Harvard Medical School Boston, Massachusetts 02115 USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/7859281$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | Alternative Splicing Amino Acid Sequence Animals Antigens, Viral - physiology B-Lymphocytes - metabolism Base Sequence cDNA Cell Line, Transformed Cell Membrane - metabolism Cytoplasm - metabolism Epstein-Barr virus Herpesvirus 4, Human - metabolism Humans LAP1 protein LMP-1 protein LMP-1-associated protein lymphocytes B man Mice Models, Biological Molecular Sequence Data nucleotide sequence Organ Specificity prediction Proteins - genetics Proteins - metabolism Receptors, Tumor Necrosis Factor - metabolism Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - metabolism RNA, Messenger - biosynthesis Sequence Homology, Amino Acid signal transduction Signal Transduction - physiology TNF Receptor-Associated Factor 1 TNF Receptor-Associated Factor 2 Viral Matrix Proteins - physiology |
| Title | The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family |
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