TY  - JOUR
AU  - Najbauer, Eszter E
AU  - Becker, Stefan
AU  - Giller, Karin
AU  - Zweckstetter, Markus
AU  - Lange, Adam
AU  - Steinem, Claudia
AU  - de Groot, Bert L
AU  - Griesinger, Christian
AU  - Andreas, Loren B
TI  - Structure, gating and interactions of the voltage-dependent anion channel.
JO  - European biophysics journal
VL  - 50
IS  - 2
SN  - 1432-1017
CY  - New York
PB  - Springer
M1  - DZNE-2021-01158
SP  - 159 - 172
PY  - 2021
AB  - The voltage-dependent anion channel (VDAC) is one of the most highly abundant proteins found in the outer mitochondrial membrane, and was one of the earliest discovered. Here we review progress in understanding VDAC function with a focus on its structure, discussing various models proposed for voltage gating as well as potential drug targets to modulate the channel's function. In addition, we explore the sensitivity of VDAC structure to variations in the membrane environment, comparing DMPC-only, DMPC with cholesterol, and near-native lipid compositions, and use magic-angle spinning NMR spectroscopy to locate cholesterol on the outside of the β-barrel. We find that the VDAC protein structure remains unchanged in different membrane compositions, including conditions with cholesterol.
KW  - Ion Channel Gating
KW  - Molecular Dynamics Simulation
KW  - Voltage-Dependent Anion Channels: chemistry
KW  - Voltage-Dependent Anion Channels: metabolism
KW  - Electrophysiology (Other)
KW  - Magic-angle spinning (Other)
KW  - Membrane protein (Other)
KW  - Molecular dynamics simulations (Other)
KW  - Solid-state NMR (Other)
KW  - Voltage dependent anion channel (Other)
LB  - PUB:(DE-HGF)16
C6  - pmid:33782728
C2  - pmc:PMC8071794
DO  - DOI:10.1007/s00249-021-01515-7
UR  - https://pub.dzne.de/record/156026
ER  -