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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。
Ubiquitination is a ubiquitous form of modification in eukaryotic cells. The modified protein molecules are involved in almost all life processes, including gene transcription, protein translation, signal transduction, cell cycle control, and growth and development. The normal function of the body play an important role. Unbalanced ubiquitin-mediated degeneration will bring a series of negative effects on the life, serious cases will lead to disease, and even life-threatening. Ubiquitin ligase E3 is the direct determinant of substrate specificity in the ubiquitination modification reaction. Its mechanism not only reveals the mystery of protein quality control and life activity function, but also provides precise control of disease-related dysregulation proteins and precision medicine Practice to provide technical support. Based on the recent progress in the study of ubiquitin ligase E3, we elucidated the specific relationship between ubiquitin ligase E3 and different types of ubiquitin chains, aiming to elucidate the molecular mechanism of protein function regulation, drug development and disease Diagnosis and treatment to provide new ideas.