The multiple assemblies of VDAC: from conformational heterogeneity to β-aggregation and amyloid formation

Biochem Soc Trans. 2016 Oct 15;44(5):1531-1540. doi: 10.1042/BST20160114.

Abstract

From their cellular localisation, to their atomic structure and their involvement in mitochondrial-driven cell death, voltage-dependent anion channels (VDACs) have challenged the scientific community with enigmas and paradoxes for over four decades. VDACs form active monomer channels in lipid bilayers, but they can also organise in multimeric assemblies. What induces, regulates and/or controls the monomer-multimer dynamics at the cellular level is not known. However, these state transitions appear to be relevant for mitochondria in making life or death decisions and for driving developmental processes. This review starts with a general introduction on VDACs and continues by examining VDAC oligomerisation/aggregation in light of recent discussions on VDAC-β-amyloid interactions and their involvement in Alzheimer's disease.

Keywords: VDAC; amyloid formation; apoptosis; oligomerisation; plants; protein aggregation.

Publication types

  • Review

MeSH terms

  • Alzheimer Disease / metabolism
  • Amyloid / chemistry*
  • Amyloid / metabolism
  • Animals
  • Humans
  • Models, Molecular
  • Protein Aggregates*
  • Protein Aggregation, Pathological*
  • Protein Conformation*
  • Protein Multimerization*
  • Voltage-Dependent Anion Channels / chemistry*
  • Voltage-Dependent Anion Channels / metabolism

Substances

  • Amyloid
  • Protein Aggregates
  • Voltage-Dependent Anion Channels