Bak and Bax are the central mediators of mitochondrial dependent programmed cell death or intrinsic apoptosis. Upon apoptotic induction, the two proteins undergo structural changes to permeabilise the mitochondrial outer membrane (MOM), thereby permitting release of cytochrome c from the mitochondrial intermembrane space. Bak is constitutively localised to the mitochondrial outer membrane where it associates with voltage dependent anion channel 2 (VDAC2) in an inactive conformation. Using blue native PAGE, inactive Bak was found to form a 440kDa complex which that is dependent on the presence of VDAC2. In addition, cells lacking VDAC2 causes an accumulation of a small but significant amount of Bak in the cytosol thus suggesting that VDAC2 is important for Bak biogenesis. Furthermore, the Bak level is substantially reduced in Vdac2-/- mouse embryonic fibroblasts (MEFs) and can be rescued by re-introduction of VDAC2 back into these cells. We find that the low level of Bak in Vdac2-/- MEFs is due to the higher turnover rate of the cytosolically accumulated form of Bak. We conclude that not only is VDAC2 important for maintaining Bak in an inactive form at mitochondria, it is also important for the efficient delivery of Bak to the mitochondrial surface.