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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October 2016
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Alternative splicing of intrinsically disordered segments can rewire protein interaction networks. In this issue, the Biochemical Society’s Colworth Medal winner, M. Madan Babu explores the contribution of intrinsically disordered regions to protein function, cellular complexity and human disease; see pages 1185–1200. [Credit: Guilhem Chalancon, MRC Laboratory of Molecular Biology, Cambridge, UK.]
Review Article|
October 19 2016
The multiple assemblies of VDAC: from conformational heterogeneity to β-aggregation and amyloid formation
Alexandre Boulbrima;
Alexandre Boulbrima
School of Applied Sciences, Department of Biological Sciences, University of Huddersfield, Queensgate, Huddersfield HD1 3DH, U.K.
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Davina Temple;
Davina Temple
School of Applied Sciences, Department of Biological Sciences, University of Huddersfield, Queensgate, Huddersfield HD1 3DH, U.K.
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Georgios Psakis
Georgios Psakis
School of Applied Sciences, Department of Biological Sciences, University of Huddersfield, Queensgate, Huddersfield HD1 3DH, U.K.
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Publisher: Portland Press Ltd
Received:
May 13 2016
Revision Received:
June 22 2016
Accepted:
June 28 2016
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2016 The Author(s); published by Portland Press Limited on behalf of the Biochemical Society
2016
Biochem Soc Trans (2016) 44 (5): 1531–1540.
Article history
Received:
May 13 2016
Revision Received:
June 22 2016
Accepted:
June 28 2016
Citation
Alexandre Boulbrima, Davina Temple, Georgios Psakis; The multiple assemblies of VDAC: from conformational heterogeneity to β-aggregation and amyloid formation. Biochem Soc Trans 15 October 2016; 44 (5): 1531–1540. doi: https://doi.org/10.1042/BST20160114
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