FBXL7 down-regulates AURKA during mitotic entry and in early mitosis|细胞周期调控数据集|蛋白质相互作用数据集

The protein levels of aurora kinase A (AURKA) during mitotic entry and in early mitosis can be reduced by the action of the SCF-FBXL7 E3 ubiquitin ligase complex consisting of SKP1, CUL1, RBX1 and FBXL7 subunits. FBXL7 is the substrate recognition subunit of the SCF-FBXL7 complex that associates with the centrosome-bound AURKA, promoting its ubiquitination and proteasome-mediated degradation. Overexpression of FBXL7 results in G2/M cell cycle arrest and apoptosis (Coon et al. 2011).<p>FBXL7 protein levels are down-regulated by the action of the SCF-FBXL18 E3 ubiquitin ligase complex, consisting of SKP1, CUL1, RBX1 and the substrate recognition subunit FBXL18. FBXL18 binds to the FQ motif of FBXL7, targeting it for ubiquitination and proteasome-mediated degradation, counteracting its pro-apoptotic activity (Liu et al. 2015). Cell cycle stage-dependency of down-regulation of FBXL7 by FBXL18 is unknown.

在细胞有丝分裂进入阶段及早期有丝分裂期间，通过SCF-FBXL7 E3泛素连接酶复合物的作用，可以降低AURKA激酶的蛋白水平。该复合物由SKP1、CUL1、RBX1和FBXL7亚基组成。FBXL7是该复合物的底物识别亚基，与着丝粒结合的AURKA相互作用，促进其泛素化和蛋白酶体介导的降解。FBXL7的过表达会导致G2/M细胞周期停滞和细胞凋亡（Coon等人，2011年）。FBXL7蛋白水平通过SCF-FBXL18 E3泛素连接酶复合物的作用而下调，该复合物由SKP1、CUL1、RBX1和底物识别亚基FBXL18组成。FBXL18与FBXL7的FQ基序结合，将其靶向泛素化和蛋白酶体介导的降解，从而抵消其促凋亡活性（Liu等人，2015年）。FBXL7由FBXL18下调的细胞周期阶段依赖性尚不明确。