摘要
Fas死亡结构域相关蛋白(Fas death domain-associated protein,DAXX)是一种高度保守的核蛋白,在细胞凋亡和转录调控中发挥重要作用。小鼠双微体基因(murine double minute 2,MDM2)是凋亡抑制家族的新成员,可通过泛素化作用调节靶蛋白活性;而泛素特异性蛋白酶7(ubiquitin-specific-processing protease 7,USP7)则通过去泛素化作用参与调节多种癌蛋白、抑癌蛋白的细胞内水平与亚细胞定位。大量文献显示MDM2的泛素化与USP7的去泛素化作用对DAXX调节的生物学活动具有重要作用,本文对DAXX此方面的研究进展做一综述。
Fas death domain-associated protein(DAXX),a highly conserved nuclear protein,plays an important role in the process of cellular apoptosis and transcription regulation.The mouse double minute 2(MDM2),a new member of the apoptosis inhibitors family(IAP),is the most potent inhibitor of apoptosis by far,which regulates target protein activity through ubiquitination;while ubiquitin-specific-processing protease 7(USP7) participates in the cellular level regulation of many cancer proteins and anticancer proteins,as well as their subcellular location,through the function of deubiquitination.Numerous studies showed that the ubiquitination and deubiquitination of MDM2 and USP7 had a great effects on the biological activities of DAXX,a summary on research progress on ubiquitination and deubiquitination of DAXX was provided.
出处
《广州化工》
CAS
2017年第13期23-25,31,共4页
GuangZhou Chemical Industry
基金
衡阳市科技局项目(2016KJ62)