论文部分内容阅读
去泛素化酶(deubiquitinating enzymes,DUBs)能对抗泛素连接酶(ubiquitin ligases),从而调节靶信号分子的泛素化和稳定性。在果蝇体内,泛素-蛋白酶体系统在调节凋亡方面发挥关键作用,最明显的是通过控制主要的凋亡调节因子——果蝇凋亡抑制蛋白1(Drosophila inhibitor of apoptosis protein 1,DIAP1)的丰度来调节凋亡。虽然基于DIAP1的泛素化机制已被广泛研究,但是DUBs在控制DIAP1活性中的确切作用仍未得到充分研究。
Deubiquitinating enzymes (DUBs) are able to antagonize ubiquitin ligases and thereby regulate the ubiquitylation and stability of target signaling molecules. In Drosophila, the ubiquitin-proteasome system plays a key role in the regulation of apoptosis, most notably by controlling the expression of the major apoptotic regulator, Drosophila inhibitor of apoptosis protein 1 (DIAP1 ) Abundance to regulate apoptosis. Although the ubiquitination mechanism based on DIAP1 has been extensively studied, the exact role of DUBs in controlling DIAP1 activity has not been well studied.