ArticleThe EMBO journal2001
CD40 and LMP-1 both signal from lipid rafts but LMP-1 assembles a distinct, more efficient signaling complex.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
40 citing papers in PubMed, 94 citations in OpenAlex.
- Targeting cholesterol-driven immunometabolism in cancer: from molecular circuits to clinical translation.Molecular cancer · 2026Review
- Understanding the role of membrane cholesterol upon Epstein Barr virus infection in astroglial cells.Frontiers in immunology · 2023Article
- Lanthanide-Based Peptide-Directed Visible/Near-Infrared Imaging and Inhibition of LMP1.JACS Au · 2021Article
- The role of trogocytosis in immune surveillance of Hodgkin lymphoma.Oncoimmunology · 2020Review
- Transmembrane Domains Mediate Intra- and Extracellular Trafficking of Epstein-Barr Virus Latent Membrane Protein 1.Journal of virology · 2018Article
- Contribution of Epstein⁻Barr Virus Latent Proteins to the Pathogenesis of Classical Hodgkin Lymphoma.Pathogens (Basel, Switzerland) · 2018Review
- CADM1 is essential for KSHV-encoded vGPCR-and vFLIP-mediated chronic NF-κB activation.PLoS pathogens · 2018Article
- The oncogenic membrane protein LMP1 sequesters TRAF3 in B-cell lymphoma cells to produce functional TRAF3 deficiency.Blood advances · 2017Article
- Roles for TNF-receptor associated factor 3 (TRAF3) in lymphocyte functions.Cytokine & growth factor reviews · 2014Review
- 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
- Epstein-Barr virus-encoded LMP1 interacts with FGD4 to activate Cdc42 and thereby promote migration of nasopharyngeal carcinoma cells.PLoS pathogens · 2012Article
- Article
- The germinal center kinase TNIK is required for canonical NF-κB and JNK signaling in B-cells by the EBV oncoprotein LMP1 and the CD40 receptor.PLoS biology · 2012Article
- Multi-Tox: application of the ToxR-transcriptional reporter assay to the study of multi-pass protein transmembrane domain oligomerization.Biochimica et biophysica acta · 2011Article
- Transmembrane peptides used to investigate the homo-oligomeric interface and binding hotspot of latent membrane protein 1.Biopolymers · 2011Article
- Characterization of the latent membrane protein 1 signaling complex of Epstein-Barr virus in the membrane of mammalian cells with bimolecular fluorescence complementation.Virology journal · 2011Article
- Canonical NF-kappaB activation is essential for Epstein-Barr virus latent membrane protein 1 TES2/CTAR2 gene regulation.Journal of virology · 2011Article
- LMP1 association with CD63 in endosomes and secretion via exosomes limits constitutive NF-κB activation.The EMBO journal · 2011Article
- Proteome-wide dysregulation by PRA1 depletion delineates a role of PRA1 in lipid transport and cell migration.Molecular & cellular proteomics : MCP · 2011Article
- The viral oncoprotein LMP1 exploits TRADD for signaling by masking its apoptotic activity.PLoS biology · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
CD40, a member of the TNFR-1 receptor family, shares several features with LMP-1, an oncoprotein encoded by Epstein-Barr virus. CD40 and LMP-1 activate transcription by binding to TRAFs, JAK3 and/or TRADD. CD40's association with CD40L activates signaling. However, LMP-1 signals independently of a ligand but dependently on self-association. We demonstrate that activated CD40 and LMP-1 co-localize in lipid rafts and recruit TRAF3 there, findings consistent with signals of CD40 and LMP-1 being initiated from lipid rafts. To elucidate their signaling, we compared requirements for their aggregation and subcellular localization. Targeting CD40's monomeric C-terminal signaling domain to lipid rafts activates signaling, as does rendering it trimeric. Addition of both modifications supports signaling more efficiently. Parallel experiments with LMP-1 indicate that targeting the monomeric C-terminal signaling domain of LMP-1 to lipid rafts activates signaling, but trimerizing it does not. Fusing LMP-1's N-terminus and membrane-spanning domains to CD40's C-terminus supports signaling more efficiently than CD40 plus ligand or CD40's trimerized and/or localized derivatives. An activity of LMP-1's N-terminus and membrane-spanning domains other than trimerization must contribute to its efficient signaling.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.