Degrons are minimal elements that mediate the interaction of proteins with degradation machineries to promote proteolysis.
蛋白降解子是调控蛋白与降解机制间相互作用并促进蛋白水解的最小元素。
Despite their central role in proteostasis, the number of known degrons remains small and a facile technology to characterize them is lacking.
尽管他们在蛋白稳态中起着重要的作用，但已知的蛋白降解子的数量仍然很少，并且缺乏识别他们的简易技术
Using a strategy combining Global Protein Stability (GPS) profiling with a synthetic human peptidome, we identify thousands of peptides containing degron activity.
使用结合全蛋白质稳定性分析和合成人类肽组的方法，我们鉴定了数千种含有降解子活性的肽
Using CRISPR screening, we established that the stability of many proteins is regulated through degrons located at their C-terminus.
使用CRISPR筛选，我们确定了许多蛋白质的稳定性是通过在它们的C末端的降解子来调节的。
We characterize eight Cullin-RING E3 ubiquitin ligase (CRL) complexes adaptors that regulate Cterminal degrons including six CRL2 and two CRL4 complexes and computationally implicate multiple non-CRLs in end recognition.
我们找到了八种调节C末端降解子的CRL复合物受体，包括6种CRL2和2种CRL4复合物，并且计算出多个非CRL受体参与末端识别
Human proteome analysis revealed that the C-termini of eukaryotic proteins are depleted for C-terminal degrons, suggesting an E3 ligase-dependent modulation of proteome composition. Thus, we propose that a series of ‘C-end rules’ operate to govern protein stability and shape the eukaryotic proteome.
人类蛋白质组分析表明，真核蛋白C末端没有C末端降解子，暗示着蛋白质组的组成依赖E3连接酶的调节。因此，我们提出了一系列C末端规则来控制蛋白质的稳定性并调节真核蛋白质组。
