Bak and Bax are the central mediators of mitochondrial dependent programmed cell death or intrinsic apoptosis. Upon apoptotic induction, the two proteins function to permeabilise the mitochondrial outer membrane (MOM), which permits for the release of cytochrome c and other apoptotic factors from the mitochondrial intermembrane space. Bak is constitutively localised to the mitochondrial outer membrane where it is found to associate with voltage dependent anion channel 2 (VDAC2). The interaction between Bak and VDACs has been reported to be crucial for restraining the pro-apoptotic activity of Bak. Using blue native PAGE, we show that the formation of a 440kDa complex containing inactive Bak is dependent on the presence of VDAC2. In addition, VDAC2, although not essential for the mitochondrial targeting process of Bak, appears to stabilise this protein at the MOM. In contrast to Bak, Bax resides in the cytosol and is only directed to mitochondria when cells undergo intrinsic apoptosis. In order to dissect the pathway of Bax regulation after the protein is anchored into mitochondria, we have utilized S184LBax, an inactive Bax mutant that is constitutively located at mitochondrial outer membrane. Our results indicate that S184LBax enters a 440kDa complex which relies on VDAC2 but not Bak expression and can be disrupted by apoptotic stimuli. Thus, the regulation of both Bak and Bax at the outer membrane appears to employ common protein components/complexes and investigation into these factors might shed light into how these pro-apoptotic molecules are controlled at the level of the mitochondria.