摘要
早幼粒白血病蛋白核体(promyelocytic leukaemia nuclear bodies,PMLNBs)是哺乳动物细胞中普遍存在的一种亚核结构,广泛参与如转录调节、基因组稳定性维持、抗病毒、细胞凋亡、肿瘤抑制等一系列的生物学事件.SUMO(smallubiquitinmodifier)修饰是蛋白质翻译后修饰领域中的研究热点,SUMO修饰对PML核体的形成与降解都发挥着重要作用.近年来研究发现,人的E3泛素连接酶RNF4(RING finger protein4),可促进依赖SUMO-2/3修饰的PML核体的泛素化连接,并且ATO(三氧化二砷)可加速其对PML核体的降解.荧光共振能量转移(fluorescence resonance energy transfer,FRET)技术可完全应用于活细胞内PML核体和SUMO蛋白之间在时间和空间上的精确互作.因此,更深入地研究PML核体形成和降解的机理以及在这个过程中重要蛋白质之间的相互作用具有重要而深远的意义.
PML NBs （promyelocytic leukaemia nuclear bodies） is subnuclear structure in mammalian cells, which widely takes part in kinds of biological events such as transcriptional regulation, genome stability, response to viral infection, apoptosis and tumor suppression. As protein post-translational modification, SUMO located in nucleus plays important roles in PML NBs formation and degradation. Recent research suggests that the human E3 ubiquitin ligase-RNF4 （RING finger protein 4）, mediates PML NBs degradation depending on SUMO-2/3 modification of PML, ATO（arsenic trioxide） could facilitate in this process. FRET（fluorescence resonance energy transfer）technology could be used in studying the protein-protein interaction of PML NBs and SUMO protein in living cells. Thus, it is far-reaching and significant to research deeply in the mechanism of the formation and degradation of PML NBs and the interaction between the important proteins during this pathway.
出处
《生物化学与生物物理进展》
SCIE
CAS
CSCD
北大核心
2010年第7期707-712,共6页
Progress In Biochemistry and Biophysics
基金
陕西省“13115”重大科技项目(2008ZDKG-068)
科技部创新基金(08C26226102378)
教育部新世纪优秀人才(NCET-08-0467)资助项目~~
作者简介
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