Approaching the structure of human VDAC1, a key molecule in mitochondrial cross-talk.

The voltage dependent anion-channel, VDAC, is the major constitutive protein of the outer membrane of mitochondria. Functionally, VDAC is involved in the exchange of small metabolites over the mitochondrial outer membrane and supports enzymes of the cytoplasm with energy precursors i.e. ATP. Moreover, the channel alone or in complex with proteins of the inner mitochondrial membrane or the intermembrane space provides a basis for docking of cytosolic proteins which can regulate outer membrane permeability in several ways. Structurally, this channel has a bacterial origin by evolution and partly resembles bacterial porin functions. However, the structure seems more complex as a variety of interactions on both channel sides can occur. Therefore, our work described is aiming to determine the structure of VDAC at atomic resolution and together with functional data to understand better how this channel can carry out such a variety of differing functions.