Allosteric regulation of BH3 proteins in Bcl-xL complexes enables switch-like activation of Bax. Bogner, C and Kale, J et al

We report here that physiologically relevant concentrations the pro-apoptotic BH3-protein Bad does not displace sufficient activator BH3-proteins from anti-apoptotic Bcl-xL to activate the pro-apoptotic protein Bax. Instead we find that Bad mediates allosteric activation of activator BH3-proteins that remain bound to Bcl-xL complexes explaining how sensitizer BH3-proteins like Bad promote switch-like activation of pro-apoptotic Bax and induce apoptosis under physiological conditions. This dataset includes images of whole western blots for Figures 2D, S2A and S4A that accompany the published manuscript.

本研究报道，在生理相关浓度下，促凋亡BH3蛋白Bad无法从抗凋亡蛋白Bcl-xL中置换出足量的激活型BH3蛋白，以激活促凋亡蛋白Bax。相反，本研究发现Bad可介导仍结合于Bcl-xL复合物的激活型BH3蛋白的变构激活，由此阐明了诸如Bad这类敏化型BH3蛋白如何在生理条件下促进促凋亡Bax的开关式激活并诱导细胞凋亡。本数据集包含已发表论文配套图表中的图2D、S2A及S4A的完整蛋白质免疫印迹（Western Blot）图像。