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.

本报告揭示了与生理学相关浓度下，促凋亡BH3蛋白Bad并不能有效置换抗凋亡Bcl-xL蛋白上的足够激活型BH3蛋白，从而激活促凋亡蛋白Bax。相反，我们发现Bad通过调节激活型BH3蛋白的变构激活，这些蛋白仍与Bcl-xL复合物结合，从而解释了促凋亡敏化型BH3蛋白如Bad如何促进促凋亡Bax的开关样激活以及在生理条件下诱导细胞凋亡。本数据集包含了图2D、S2A和S4A的完整Western印迹图像，这些图像与已发表的论文相伴随。