ArticleThe EMBO journal2006
PRA1 promotes the intracellular trafficking and NF-kappaB signaling of EBV latent membrane protein 1.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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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
29 citing papers in PubMed, 42 citations in OpenAlex.
- Shigella Effector VirA Suppresses Plant Immunity by Compromising PRA1.F3-Dependent Accumulation of FLS2 at the Plasma Membrane.Plant, cell & environment · 2026Article
- 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
- ADP ribosylation factor-like GTPase 6-interacting protein 5 (Arl6IP5) is an ER membrane-shaping protein that modulates ER-phagy.The Journal of biological chemistry · 2025Article
- Epstein-Barr virus latent membrane protein-1 upregulates autophagy and promotes viability in Hodgkin lymphoma: Implications for targeted therapy.Cancer science · 2021Article
- Di-arginine and FFAT-like motifs retain a subpopulation of PRA1 at ER-mitochondria membrane contact sites.PloS one · 2020Article
- Epstein-Barr virus subverts mevalonate and fatty acid pathways to promote infected B-cell proliferation and survival.PLoS pathogens · 2019Article
- In silico evidence of de novo interactions between ribosomal and Epstein - Barr virus proteins.BMC molecular and cell biology · 2019Article
- The Hippo Pathway and Viral Infections.Frontiers in microbiology · 2019Review
- 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
- Tomato Prenylated RAB Acceptor Protein 1 Modulates Trafficking and Degradation of the Pattern Recognition Receptor LeEIX2, Affecting the Innate Immune Response.Frontiers in plant science · 2018Article
- Positive regulation of TAZ expression by EBV-LMP1 contributes to cell proliferation and epithelial-mesenchymal transition in nasopharyngeal carcinoma.Oncotarget · 2017Article
- The Prenylated Rab GTPase Receptor PRA1.F4 Contributes to Protein Exit from the Golgi Apparatus.Plant physiology · 2017Article
- Characterization of the rapamycin-inducible EBV LMP1 activation system.Journal of microbiology (Seoul, Korea) · 2015Article
- A Review: Proteomics in Nasopharyngeal Carcinoma.International journal of molecular sciences · 2015Review
- Exosomal sorting of the viral oncoprotein LMP1 is restrained by TRAF2 association at signalling endosomes.Journal of extracellular vesicles · 2015Article
- Article
- Review
- A role for prenylated rab acceptor 1 in vertebrate photoreceptor development.BMC neuroscience · 2012Article
- Genome-wide RNAi screening identifies human proteins with a regulatory function in the early secretory pathway.Nature cell biology · 2012Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Latent membrane protein 1 (LMP1), which is an Epstein-Barr virus (EBV)-encoded oncoprotein, induces nuclear factor-kappa B (NF-kappaB) signaling by mimicking the tumor necrosis factor receptor (TNFR). LMP1 signals primarily from intracellular compartments in a ligand-independent manner. Here, we identify a new LMP1-interacting molecule, prenylated Rab acceptor 1 (PRA1), which interacts with LMP1 for the first time through LMP1's transmembrane domain, and show that PRA1 is involved in intracellular LMP1 trafficking and LMP1-induced NF-kappaB activity. Immunofluorescence and biochemical analyses revealed that LMP1 physically interacted with PRA1 at the Golgi apparatus, and the colocalization of LMP1 and PRA1 to the Golgi was sensitive to nocodazole and brefeldin A. Coexpression of a PRA1 export mutant or knockdown of PRA1 led to redistribution of LMP1 and its associated signaling molecules to the endoplasmic reticulum and subsequent impairment of LMP1-induced NF-kappaB activation, but had no effect on CD40- and TNFR1-mediated signaling or the functional integrity of the Golgi apparatus. These novel findings provide important new insights into LMP1, and identify an unexpected new role for PRA1 in cellular 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.