Assessing the role of residue E73 and lipid headgroup charge in VDAC1 voltage gating.

ABSTRACT: The voltage-dependent anion channel (VDAC) is the most abundant protein of the mitochondrial outer membrane (MOM) where it regulates transport of ions and metabolites in and out of the organelle. VDAC function is extensively studied in a lipid bilayer system that allows conductance monitoring of reconstituted channels under applied voltage. The process of switching from a high-conductance state, open to metabolites, to a variety of low-conducting states, which excludes metabolite transport, is termed voltage gating and the mechanism remains poorly understood. Recent studies have implicated the involvement of the membrane-solvated residue E73 in the gating process through β-barrel destabilization. However, there has been no direct experimental evidence of E73 involvement in VDAC1 voltage ga

SUBMITTER: Queralt-Martin M 

PROVIDER: S-EPMC8283775 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature