据2013年6月4日张召(Dev Cell,2013 Jun 4.doi:10.1016/j.devcel.2013.05.006)报道,中国学者发现,Ter94复合物选择K11连接形式泛素(ubiquitin)化修饰的Ci蛋白被蛋白酶体(proteasome)部分降解。蛋白质的泛素化降解作为一个重要的调控机制参与了细胞内的多种生命活动。在这个过程中,蛋白质本身会被加上一种叫做泛素的小分子修饰,形成泛素链,从而作为标签被蛋白酶体识别降解。 According to a report by Dev Zhao (2013 Jun 4. doi: 10.1016 / j.devcel.2013.05.006) on June 4, 2013, Chinese researchers found that the Ter94 complex chose a K11-linked ubiquitin-modified Ci protein is partially degraded by the proteasome. Ubiquitination degradation of protein is involved in a variety of life activities in the cell as an important regulatory mechanism. In the process, the protein itself is added with a small molecule called ubiquitin to form an ubiquitin chain, which is then used as a tag to recognize and degrade proteasomes.