期刊
JOURNAL OF GENERAL VIROLOGY
卷 89, 期 -, 页码 2437-2446出版社
MICROBIOLOGY SOC
DOI: 10.1099/vir.0.2008/003897-0
关键词
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资金
- National Science Council of the Republic of China [NSC96-3112-B-182-002, NSC95-2320-B-182-041-MY3]
- National Health Research Institute of the Republic of China [NHRI-EX96-9417BI]
- Chang-Gung Molecular Medicine Research Center [CMRPD160111]
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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