爱泼斯坦-巴尔病毒早期即刻蛋白Rta对ERK信号转导通路的激活作用
Activation of the ERK signal transduction pathway by Epstein-Barr virus immediate-early protein Rta.
作者信息
Lee Yu-Hsiu, Chiu Ya-Fang, Wang Wen-Hung, Chang Li-Kwan, Liu Shih-Tung
机构信息
Institute of Microbiology and Immunology, National Yang-Ming University, 155 Linong Street Section 2, Taipei 112, Taiwan, ROC.
Molecular Genetics Laboratory, Department of Microbiology and Immunology, Chang-Gung University, 259 Wen-Hua 1st Road, Kwei-Shan, Taoyuan 333, Taiwan, ROC.
出版信息
J Gen Virol. 2008 Oct;89(Pt 10):2437-2446. doi: 10.1099/vir.0.2008/003897-0.
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.
已知乳腺癌1号关联蛋白2（BRAP2）与Ras 1激酶抑制因子（KSR1）相互作用，抑制细胞外信号调节激酶（ERK）信号转导级联反应。本研究发现，爱泼斯坦-巴尔病毒（EBV）的即刻早期蛋白Rta是BRAP2在酵母中的结合伙伴，并通过谷胱甘肽S-转移酶下拉试验在体外证实了这种结合，且在293（maxi-EBV）细胞中通过免疫共沉淀在体内证实了这种结合。结合研究还表明，Rta和KSR1与BRAP2的C末端202个氨基酸区域相互作用。此外，Rta似乎会阻止KSR1与BRAP2的结合，激活ERK信号转导通路以及EBV即刻早期基因BZLF1的转录。Rta对ERK信号转导通路的激活可能对维持EBV的裂解状态至关重要。
Zotero 插件