title: Characterization of the rapamycin-inducible EBV LMP1 activation system.
abstract: Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1) is required for EBV-mediated B lymphocyte transformation into proliferating lymphoblastoid cell lines (LCL). LMP1 oligomerizes spontaneously in membrane lipid rafts via its transmembrane domain and constitutively activates signal transduction pathways, including NF-κB, p38 Mitogen-Activated Protein Kinase (MAPK), and c-Jun N-terminal Kinase (JNK). Since LMP1 mimics the tumor necrosis factor receptor (TNFR), CD40, it may be effectively utilized to study the effects of constitutive activation of signal transduction pathways on cellular physiology. On the other hand, LMP1 presents a disadvantage in terms of determining the sequential events and factors involved in signaling pathways. A CD40-LMP1 chimeric molecule has been generated to overcome this limitation but does not represent the authentic and physiological nature of LMP1. In the current study, a ligand-dependent activation system for LMP1 using rapamycin-inducible dimerization was generated to delineate the LMP1 signaling pathway.
authors.affiliation: Department of Life Science, Gachon University, Seongnam, 13120, Republic of Korea.
authors.forename: Sang Yong
authors.initials: SY
authors.lastname: Kim
authors.affiliation: Department of Life Science, Gachon University, Seongnam, 13120, Republic of Korea.
authors.forename: Jung-Eun
authors.initials: JE
authors.lastname: Kim
authors.affiliation: Department of Life Science, Gachon University, Seongnam, 13120, Republic of Korea.
authors.forename: Jiyeon
authors.initials: J
authors.lastname: Won
authors.affiliation: Department of Life Science, Gachon University, Seongnam, 13120, Republic of Korea. songyj@gachon.ac.kr.
authors.forename: Yoon-Jae
authors.initials: YJ
authors.lastname: Song
mesh_terms: D002352:Carrier Proteins; D002462:Cell Membrane / Q000378:metabolism; D017931:DNA Primers; D015870:Gene Expression / Q000187:drug effects; D057809:HEK293 Cells; D004854:Herpesvirus 4, Human / Q000187:drug effects / Q000235:genetics* / Q000378:metabolism*; D006801:Humans; D016328:NF-kappa B / Q000378:metabolism; D055503:Protein Multimerization; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction / Q000187:drug effects; D020123:Sirolimus / Q000494:pharmacology*; D058570:TOR Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism; D022021:Tacrolimus Binding Proteins / Q000235:genetics / Q000378:metabolism; D014763:Viral Matrix Proteins / Q000235:genetics* / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D017931:DNA Primers; C037662:EBV-associated membrane antigen, Epstein-Barr virus; D016328:NF-kappa B; D011993:Recombinant Fusion Proteins; D014763:Viral Matrix Proteins; C546842:MTOR protein, human; D058570:TOR Serine-Threonine Kinases; D022021:Tacrolimus Binding Proteins; D020123:Sirolimus
keywords: Epstein-Barr virus; NF-κB; latent membrane protein 1