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.
Steps to reproduce
Please see the methods from the published manuscript