- Characterization of the rapamycin-inducible EBV LMP1 activation system
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Sang Yong Kim , Jung-Eun Kim , Jiyeon Won , Yoon-Jae Song
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J. Microbiol. 2015;53(10):732-738. Published online October 2, 2015
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DOI: https://doi.org/10.1007/s12275-015-5455-z
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 Abstract
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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.
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