Lee, Yu-HsiuYu-HsiuLeeChiu, Ya-FangYa-FangChiuWang, Wen-HungWen-HungWangChang, Li-KwanLi-KwanChangLiu, Shih-TungShih-TungLiu2009-07-222018-07-062009-07-222018-07-06200800221317http://ntur.lib.ntu.edu.tw//handle/246246/162437BRCA1-associated protein 2 (BRAP2) is known to interact with the kinase suppresson 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 coimmunoprecipitation 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.application/pdf495441 bytesapplication/pdfen-US10.1099/vir.0.2008/003897-0http://ntur.lib.ntu.edu.tw/bitstream/246246/162437/1/04.pdf