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

Published: 20 November 2019| Version 1 | DOI: 10.17632/cnpr3w25sy.1
Justin Kale


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.


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Sunnybrook Research Institute


Western Blot