ArticleProceedings of the National Academy of Sciences of the United States of America2004
Latent infection membrane protein transmembrane FWLY is critical for intermolecular interaction, raft localization, and signaling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 70 citations in OpenAlex.
- A CRISPR-Cas9 screen Reveals STEEP1 as a Key Host Dependency Factor for Epstein-Barr Virus Latent Membrane Protein 1 Trafficking and Signaling.bioRxiv : the preprint server for biology · 2026Article
- Disruption of ATR Signaling by Epstein-Barr Virus Latent Membrane Protein 1 Sensitizes Nasopharyngeal Carcinoma Cells to Cisplatin.Journal of medical virology · 2025Article
- Epstein-Barr virus-infected nasopharyngeal carcinoma therapeutics: oncoprotein targets and clinical implications.Medical oncology (Northwood, London, England) · 2025Review
- Paradoxical effects of DNA tumor virus oncogenes on epithelium-derived tumor cell fate during tumor progression and chemotherapy response.Signal transduction and targeted therapy · 2021Article
- New Look of EBV LMP1 Signaling Landscape.Cancers · 2021Review
- Lanthanide-Based Peptide-Directed Visible/Near-Infrared Imaging and Inhibition of LMP1.JACS Au · 2021Article
- Dual-Targeting Peptide-Guided Approach for Precision Delivery and Cancer Monitoring by Using a Safe Upconversion Nanoplatform.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- The Epstein-Barr virus LMP1 interactome: biological implications and therapeutic targets.Future virology · 2018Article
- Transmembrane Domains Mediate Intra- and Extracellular Trafficking of Epstein-Barr Virus Latent Membrane Protein 1.Journal of virology · 2018Article
- Review
- Article
- Signaling by the Epstein-Barr virus LMP1 protein induces potent cytotoxic CD4Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- CD63 Regulates Epstein-Barr Virus LMP1 Exosomal Packaging, Enhancement of Vesicle Production, and Noncanonical NF-κB Signaling.Journal of virology · 2017Article
- A novel recombinant variant of latent membrane protein 1 from Epstein Barr virus in Argentina denotes phylogeographical association.PloS one · 2017Article
- Constitutively Active MAVS Inhibits HIV-1 Replication via Type I Interferon Secretion and Induction of HIV-1 Restriction Factors.PloS one · 2016Article
- TRAF1 Coordinates Polyubiquitin Signaling to Enhance Epstein-Barr Virus LMP1-Mediated Growth and Survival Pathway Activation.PLoS pathogens · 2015Article
- Epstein-Barr virus latent genes.Experimental & molecular medicine · 2015Review
- Exosomal sorting of the viral oncoprotein LMP1 is restrained by TRAF2 association at signalling endosomes.Journal of extracellular vesicles · 2015Article
- High molecular weight complex analysis of Epstein-Barr virus Latent Membrane Protein 1 (LMP-1): structural insights into LMP-1's homo-oligomerization and lipid raft association.Virus research · 2013Article
- Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Relatively little is known about the biochemical mechanisms through which the Epstein-Barr virus latent infection integral membrane protein 1 (LMP1) transmembrane domains cause constitutive LMP1 aggregation and continuous cytoplasmic C terminus-mediated signal transduction. We now evaluate the role of the three consecutive LMP1 hydrophobic transmembrane pairs, transmembrane domains (TM)1-2, TM3-4, and TM5-6, in intermolecular aggregation and NF-kappaB activation. LMP1TM1-2 enabled approximately 40% of wild-type LMP1 cytoplasmic domain-mediated NF-kappaB activation, whereas TM3-4 or TM5-6 assayed in parallel had almost no effect independent of LMP1TM1-2. Alanine mutagenesis of conserved residues in LMP1TM1-2 identified FWLY(38-41) to be critical for LMP1TM1-2 intermolecular association with LMP1TM3-6. Further, in contrast to wild-type LMP1, LMP1 with FWLY(38-41) mutated to AALA(38-41) did not (i). significantly partition to lipid Rafts or Barges and effectively intermolecularly associate, (ii). enable cytoplasmic C terminus engagement of tumor necrosis factor receptor-associated factor 3, (iii). activate NF-kappaB, and thereby (iv). induce tumor necrosis factor receptor-associated factor 1 expression. Other LMP1 intermolecular associations were observed that involved LMP1TM1-2/LMP1TM1-2 or LMP1TM3-4/LMP1TM3-6 interactions; these probably also contribute to LMP1 aggregation. Because FWLY(38-41) was essential for LMP1-mediated signal transduction, and LMP1 activation of NF-kappaB is essential for proliferating B lymphocyte survival, inhibition of LMP1FWLY(41)-mediated LMP1/LMP1 intermolecular interactions is an attractive therapeutic target.
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