The Outer Mitochondrial Membrane Pore (Voltage‐Dependent Anion Channel)

Abstract

Originally published in: Bacterial and Eukaryotic Porins. Edited by Roland Benz. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30775‐3 The sections in this article are Introduction Structure and Isotypes of VDAC The Influence of Phospholipids on VDAC Structure VDAC Conductance and Ion Selectivity Physiological Significance of the Voltage Dependence Porins as Specific Binding Sites VDAC senses Inner Membrane Functions in the Contact Site Cytochrome c is a Component of the Contact Sites Isolation and Characterization of VDAC‐ANT Complexes Reconstitution of VDAC‐ANT Complexes Importance of Metabolic Channeling in Regulation of Energy Metabolism The VDAC‐ANT Complex as Permeability Transition Pore The VDAC‐ANT Complex as a Target for Bax‐dependent Cytochrome c Release The VDAC–ANT Complexes contain Cytochrome c The Importance of the Kinases in Regulation of Apoptosis Suppression of Bax‐dependent Cytochrome c Release and Permeability Transition by Hexokinase Suppression of Permeability Transition by Mitochondrial Creatine Kinase Conclusion