VDAC-1 (outer mitochondrial membrane protein porin 1) is a voltage dependent anion channel that mediates the flow of metabolites and ions across the outer mitochondrial membrane. VDAC-1 appeares to be a pro-apoptotic protein through oligomerisation []. It is implicated in cell death induction for its ability to interact with BAX, a protein belonging to the BCL-2 protein family. BAX plays a role in apoptosis and mitochondrial function regulation via multiple protein-protein interactions with BCL-2, BAK, BID or other members of the family [, ]. Voltage dependent anion channels (VDACs) or porins by analogy with bacterial porins, are pore-forming proteins associated with mitochondria, although they are also present in the endoplasmic reticulum (ER) []and plasma membrane []. In mammals, three VDAC isoforms have been identified: VDAC1 to 3. They have a very similar predicted structure, consisting of a 19 amphipathic β-strands barrel with an N-terminal α-helix in the central pore [, ]. The channel opening faces both the cytosol and mitochondrial intermembrane space [, ]. They play a major role in cellular energetic metabolism due to its ability to allow the exchange of molecules between the cytosol and the mitochondrial intermembrane space. They may also play a role in cell death. However, several mouse gene knock out studies show that VDACs are dispensable for both MPT (mitochondrial permeability transition) and Bcl-2 family member-driven cell death [, ].
This entry includes VDAC3 from animals. Recombinant VDAC3 shows a channel activity with a very small conductance []. VDAC3 is involved in the transport of ADP across the mitochondrial outer membrane in the cardiac muscle (oxidative muscle) but not in the gastrocnemius muscle (mixed muscle) []. VDAC3 is also a centrosomal protein that interacts with the centrosomal protein kinase Mps1 []. VDAC3 and Mps1 negatively regulate ciliogenesis; they promote ciliary disassembly during cell cycle entry and suppress cilia assembly in proliferating cells []. Mice lacking VDAC3 suffered from immotile sperm and infertility [].Voltage dependent anion channels (VDACs) or porins by analogy with bacterial porins, are pore-forming proteins associated with mitochondria, although they are also present in the endoplasmic reticulum (ER) []and plasma membrane []. In mammals, three VDAC isoforms have been identified: VDAC1 to 3. They have a very similar predicted structure, consisting of a 19 amphipathic β-strands barrel with an N-terminal α-helix in the central pore [, ]. The channel opening faces both the cytosol and mitochondrial intermembrane space [, ]. They play a major role in cellular energetic metabolism due to its ability to allow the exchange of molecules between the cytosol and the mitochondrial intermembrane space. They may also play a role in cell death. However, several mouse gene knock out studies show that VDACs are dispensable for both MPT (mitochondrial permeability transition) and Bcl-2 family member-driven cell death [, ].
VDAC2 is a voltage dependent anion channel that mediates the flow of metabolites and ions across the outer mitochondrial membrane. It may play a role in mitochondrial apoptosis through its involvement in the mitochondrial recruitment of BAK, a protein belonging to the BCL-2 protein family [, , ].Voltage dependent anion channels (VDACs) or porins by analogy with bacterial porins, are pore-forming proteins associated with mitochondria, although they are also present in the endoplasmic reticulum (ER) []and plasma membrane []. In mammals, three VDAC isoforms have been identified: VDAC1 to 3. They have a very similar predicted structure, consisting of a 19 amphipathic β-strands barrel with an N-terminal α-helix in the central pore [, ]. The channel opening faces both the cytosol and mitochondrial intermembrane space [, ]. They play a major role in cellular energetic metabolism due to its ability to allow the exchange of molecules between the cytosol and the mitochondrial intermembrane space. They may also play a role in cell death. However, several mouse gene knock out studies show that VDACs are dispensable for both MPT (mitochondrial permeability transition) and Bcl-2 family member-driven cell death [, ].
