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1 Institute of Microbiology and Immunology, National Yang-Ming University, 155 Linong Street Section 2, Taipei 112, Taiwan, ROC
2 Molecular Genetics Laboratory, Department of Microbiology and Immunology, Chang-Gung University, 259 Wen-Hua 1st Road, Kwei-Shan, Taoyuan 333, Taiwan, ROC
3 Institute of Microbiology and Biochemistry, National Taiwan University, 1 Roosevelt Road Section 4, Taipei 106, Taiwan, ROC
Correspondence
Shih-Tung Liu
cgliu{at}mail.cgu.edu.tw
BRCA1-associated protein 2 (BRAP2) is known to interact with the kinase suppressor of Ras 1 (KSR1), inhibiting the ERK signal transduction cascade. This study found that an Epstein–Barr virus (EBV) immediate-early protein, Rta, is a binding partner of BRAP2 in yeast and confirmed the binding in vitro by a glutathione S-transferase pull-down assay and in vivo by co-immunoprecipitation in 293(maxi-EBV) cells. Binding studies also showed that Rta and KSR1 interacted with the C-terminal 202 aa region in BRAP2. Additionally, Rta appeared to prevent the binding of KSR1 to BRAP2, activating the ERK signal transduction pathway and the transcription of an EBV immediate-early gene, BZLF1. Activation of the ERK signal transduction pathway by Rta may be critical for the maintenance of the lytic state of EBV.
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