中国科技核心期刊
CN:31-1600/Q
ISSN:1004-0374
基因编辑学术研讨会(2017)      关于有网站冒充本刊网站的声明      2017(第四届)基因编辑与临床应用研讨会      2017新型生物标志物发现与应用研讨会
《生命科学》 2017, 29(8): 722-731
泛素连接酶E3与泛素链修饰类型特异性研究进展
陈 杨,王富强,徐 平*
(军事医学科学院放射与辐射医学研究所,国家蛋白质科学中心(北京),北京蛋白质组研究中心,蛋白质组学国家重点实验室,北京 102206)
摘 要:泛素化修饰是真核细胞内广泛存在的一种修饰形式,受到该修饰的蛋白质分子遍及基因转录、蛋白质翻译、信号转导、细胞周期控制以及生长发育等几乎所有的生命活动过程,对生命体正常功能的发挥具有重要作用。泛素化修饰的失调会给生命体带来一系列负面影响,严重者将导致疾病,甚至危及生命。泛素连接酶E3 是泛素化修饰反应中底物特异性的直接决定者,其机制研究不仅可揭示蛋白质质量控制和生命活动功能的奥秘,也将为疾病关联失调蛋白的精准调控和精准医学实践提供技术支撑。现结合当前对泛素连接酶E3 研究的最新进展,阐述泛素连接酶E3 发挥作用时与不同类型泛素链之间的特异性关系,旨在为蛋白质功能调控的分子机制、药物研制和疾病诊治提供新思路。
 
Progress in the specificity of ubiquitin ligase for ubiquitin chains
CHEN Yang, WANG Fu-Qiang, XU Ping*
(State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences (Beijing), Beijing Institute of Radiation Medicine, Beijing 102206, China)
Abstract: Ubiquitination is one of the most widely existed protein post-translational modification in eukaryotic cells which is involved in many biological processes including transcription, translation, signal transduction, cell cycle control, and growth and development. Disturbance of the ubiquitin system would bring a series of negative effects to the living body and, more seriously, could lead to severe diseases or even death. E3 ubiquitin ligases confer substrate specificity of ubiquitin modification by interacting with substrate proteins directly. Exploring their mechanisms would make a great contribution on understanding the regulation of protein in cells, and finally to precision medicine. Here, we systematically reviewed the most recent advances in E3 ubiquitin ligases study, and discussed the specific relationship between E3 ubiquitin ligases and different types of ubiquitin chains, aiming to provide new ideas for disease therapy and drug target selection.
 
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