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出 处:《医学分子生物学杂志》2005年第6期452-455,共4页Journal of Medical Molecular Biology
基 金:国家自然科学基金(No.39525022)
摘 要:泛素-蛋白酶体途径是真核细胞内重要的蛋白质调控系统,参与调节细胞周期进程、细胞增生与分化,以及信号传导等多种细胞生理过程,因此,细胞内蛋白泛素化降解是蛋白质重要的转录后修饰方式。EBV编码多种病毒蛋白,通过泛素.蛋白酶体途径调节病毒的潜伏,使病毒能在免疫活性较高的宿主体中存活。LMP1和LMP2A可能作为泛素.蛋白酶体途径的底物而受其调控,EBNA1则充当蛋白酶体降解过程中的阻滞剂。对它们在该途径中不同作用的深入了解将促使我们发展治疗EBV相关癌症的新策略。The ubiquititn-proteasome pathway was an important protein regulation system in eukaryotic cells, which was involved in various cell processes such as the regulation of cell cycle, proliferation and differentiation of cells, and signal transduction. Therefore, the protein degradation by ubiquitin-proteasome in cells serves as an essential post-transcription modification pathway. EBV encodes several proteins that exploit the ubiquitin-proteasome system to regulate latency and allow the persistence of infected cells in immunocompetent hosts. We disscussed the interaction mechanism of ubiquitin-proteasom system with the three proteins encoded by EBV including LMP1, LMP2A and EBNA1. The better understanding of the pathway can help us develop a novel therapy strategy for EBV-related caucer.
关 键 词:EPSTEIN-BARR病毒 蛋白质调控 泛素-蛋白酶体途径
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