Wu Chu-Chiao, Bratton Shawn B
Department of Epigenetics and Molecular Carcinogenesis, The University of Texas MD Anderson Cancer Center , Smithville, TX, USA.
Mol Cell Oncol. 2017 Jan 20;4(2):e1281865. doi: 10.1080/23723556.2017.1281865. eCollection 2017.
For nearly 2 decades, investigators have debated whether cysteinyl-aspartate-specific protease 9 (caspase-9) is activated within the apoptotic protease-activating factor 1 (Apaf-1) apoptosome through proximity-induced homodimerization or through formation of a holoenzyme. Recently, we have demonstrated that caspase-9 forms (and likely transitions between) both caspase-9 homo- and Apaf-1:caspase-9 heterodimers, each of which plays unique roles in the recruitment and activation of caspase-9.
近20年来,研究人员一直在争论半胱天冬酶9(caspase-9)是通过邻近诱导的同源二聚化还是通过全酶的形成在凋亡蛋白酶激活因子1(Apaf-1)凋亡小体中被激活。最近,我们已经证明caspase-9形成了caspase-9同源二聚体以及Apaf-1:caspase-9异源二聚体(并且可能在两者之间转换),每一种二聚体在caspase-9的募集和激活中都发挥着独特作用。