During apoptosis, the BCL-2-family protein tBID promotes mitochondrial permeabilization by activating BAX and BAK and by blocking anti-apoptotic BCL-2 members. Here, the researchers report that tBID can also mediate mitochondrial permeabilization by itself, resulting in the release of cytochrome c and mitochondrial DNA, caspase activation and apoptosis even in absence of BAX and BAK. Importantly, this mechanism is physiologically relevant in the immune response against Shigella infection. Furthermore, it can be exploited to kill leukaemia cells with acquired venetoclax resistance due to the lack of active BAX and BAK. These findings define tBID as an effector of mitochondrial permeabilization in apoptosis and provide a new paradigm for BCL-2 proteins, with implications for anti-bacterial immunity and cancer therapy.
BCL-2-family protein tBID can act as a BAX-like effector of apoptosis
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