BAD association with membranes is regulated by Raf kinases and association with 14-3-3 proteins

Using a set of specific kinase inhibitors we demonstrate that Raf kinases phosphorylate BAD at serines 112, 136 and 155 in vivo and in vitro. Exploring unexpected lipid binding properties of BAD we identified two lipid-binding domains located in its C-terminal part. Furthermore, we believe to have uncovered how phosphorylation-driven interaction with 14-3-3 regulates intracellular membrane localization of BAD. Observed activity of lipid-bound BAD as a membrane receptor for Bcl-XL opens new horizons in apoptosis research.