The multiple assemblies of VDAC

From conformational heterogeneity to β-aggregation and amyloid formation

Alexandre Boulbrima, Davina Temple, Georgios Psakis

Research output: Contribution to journalReview article

2 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1531-1540
Number of pages10
JournalBiochemical Society Transactions
Volume44
Issue number5
DOIs
Publication statusPublished - 15 Oct 2016

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Voltage-Dependent Anion Channels
Amyloid
Agglomeration
Monomers
Oligomerization
Mitochondria
Lipid bilayers
Lipid Bilayers
Cell death
Alzheimer Disease
Cell Death

Cite this

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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.",
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The multiple assemblies of VDAC : From conformational heterogeneity to β-aggregation and amyloid formation. / Boulbrima, Alexandre; Temple, Davina; Psakis, Georgios.

In: Biochemical Society Transactions, Vol. 44, No. 5, 15.10.2016, p. 1531-1540.

Research output: Contribution to journalReview article

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