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Structure, gating and interactions of the voltage-dependent anion channel.

ABSTRACT: 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.

SUBMITTER: Najbauer EE

PROVIDER: S-EPMC8071794 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature

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Structure, gating and interactions of the voltage-dependent anion channel.

Najbauer Eszter E EE Becker Stefan S Giller Karin K Zweckstetter Markus M Lange Adam A Steinem Claudia C de Groot Bert L BL Griesinger Christian C Andreas Loren B LB

European biophysics journal : EBJ 20210329 2

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 ...[more]

PMID: 33782728

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