德隆
生物
泛素
泛素蛋白连接酶类
细胞生物学
泛素连接酶
蛋白质水解
核糖体
蛋白质降解
计算生物学
生物化学
作者
Dawafuti Sherpa,Jakub Chrustowicz,Brenda A. Schulman
出处
期刊:Molecular Cell
[Elsevier]
日期:2022-03-01
卷期号:82 (8): 1424-1438
被引量:3
标识
DOI:10.1016/j.molcel.2022.02.004
摘要
Specificity of eukaryotic protein degradation is determined by E3 ubiquitin ligases and their selective binding to protein motifs, termed "degrons," in substrates for ubiquitin-mediated proteolysis. From the discovery of the first substrate degron and the corresponding E3 to a flurry of recent studies enabled by modern systems and structural methods, it is clear that many regulatory pathways depend on E3s recognizing protein termini. Here, we review the structural basis for recognition of protein termini by E3s and how this recognition underlies biological regulation. Diverse E3s evolved to harness a substrate's N and/or C terminus (and often adjacent residues as well) in a sequence-specific manner. Regulation is achieved through selective activation of E3s and also through generation of degrons at ribosomes or by posttranslational means. Collectively, many E3 interactions with protein N and C termini enable intricate control of protein quality and responses to cellular signals.
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