ArticleVirology journal2011
Characterization of the latent membrane protein 1 signaling complex of Epstein-Barr virus in the membrane of mammalian cells with bimolecular fluorescence complementation.
Article in Virology journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- The Epstein-Barr virus LMP1 interactome: biological implications and therapeutic targets.Future virology · 2018Article
- Review
- Regulation of Latent Membrane Protein 1 Signaling through Interaction with Cytoskeletal Proteins.Journal of virology · 2015Article
- Identification of transmembrane protein 134 as a novel LMP1-binding protein by using bimolecular fluorescence complementation and an enhanced retroviral mutagen.Journal of virology · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundBimolecular fluorescence complementation (BiFC) is a novel technique to examine protein-protein interaction through the assembly of fluorescent proteins. In the present study, BiFC was used to study the assembly of the Epstein-Barr virus latent membrane protein 1 (LMP1) signaling complex within the membrane of mammalian cells. LMP1 signaling requires oligomerization, localization to lipid rafts, and association of the cytoplasmic domain to adaptor proteins, such as the tumor necrosis factor receptor associated factors (TRAFs).
methodsLMP1-TRAF and LMP1-LMP1 interactions were assayed by BiFC using fluorescence microscopy and flow cytometry. Function of LMP1 BiFC contructs were confirmed by transformation assays and nuclear factor- κB (NF-κB) reporter assays.
resultsBiFC was observed between LMP1 and TRAF2 or TRAF3 and mutation of the LMP1 signaling domains reduced complementation. Fluorescence was observed in previously described LMP1 signaling locations. Oligomerization of LMP1 with itself induced complementation and BiFC. LMP1-BiFC constructs were fully functional in rodent fibroblast transformation assays and activation of NF-κB reporter activity. The BiFC domain partially suppressed some LMP1 mutant phenotypes.
conclusionsTogether these data suggest that BiFC is a unique and novel platform to identify and characterize proteins recruited to the LMP1-signaling complex.
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