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On the mechanism and functional significance of the ADP/ATP carrier (AAC) dimerization

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Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology Aims and scope

Abstract

According to previous studies, ADP/ATP carrier (AAC) can possibly exist as a monomer or in a dimer state in the inner mitochondrial membrane; however, the question on its functional oligomeric state is still open. The aim of the present work is to establish the external factors that could control the functional oligomeric state of AAC (i.e., monomer or dimer). The study is based on the results of our previous work, which revealed that the volume regulation system of mitochondria (MVRS) affects the oxidative phosphorylation (OXPHOS) system: MVRS could transfer OXPHOS system functioning in a state of supercomplex. Consequently, one may expect that the volume regulation system could also control the functional state of AAC during phosphorylation. Here, on rat liver mitochondria we show that, depending on the incubation medium tonicity, AAC functions in two different ways: either as a monomer (in hypotonic and isotonic media) or as a dimer (in a hypertonic medium). Thus, the transition between the monomeric and dimeric forms of AAC is regulated by MVRS, as well as by functioning of OXPHOS. We conclude that the structural reorganization of AAC is associated with the entire OXPHOS reorganization into a supercomplex. It was also found that dimerization of AAC can occur not only due to the action of MVRS (in hypotonic media) but also under hypoxic conditions.

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Abbreviations

MVRS:

mitochondrial volume regulation system

AAC:

ADP/ATP carrier

OXPHOS:

oxidative phosphorylation

SAN:

small angle neutron scattering

EM:

electron microscopy

CATR:

carboxyatractyloside

HEPES:

4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid)

EDTA:

ethylenediaminetetraacetic acid

BSA:

bovine serum albumin

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Author notes

  1. These authors equally contributed to the work.

Authors and Affiliations

  1. Institut de Biologie Structurale (IBS), University Grenoble Alpes, CEA, CNRS, 38044, Grenoble, France

    V. S. Moiseeva, S. Ravaud, V. I. Gordeliy & E. Pebay-Peyroula

  2. Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research, Dubna, 141980, Russia

    T. N. Murugova

  3. Moscow Institute of Physics and Technology, Dolgoprudny, 141701, Russia

    T. N. Murugova, I. M. Byvshev, V. I. Gordeliy & L. S. Yaguzhinsky

  4. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119992, Russia

    I. M. Vangeli, R. A. Simonyan & L. S. Yaguzhinsky

  5. Institute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Research Centre Juelich, 52425, Juelich, Germany

    V. I. Gordeliy

Authors
  1. V. S. Moiseeva
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  2. T. N. Murugova
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  3. I. M. Vangeli
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  4. I. M. Byvshev
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  5. S. Ravaud
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  6. R. A. Simonyan
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  7. V. I. Gordeliy
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  8. E. Pebay-Peyroula
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  9. L. S. Yaguzhinsky
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Corresponding author

Correspondence to L. S. Yaguzhinsky.

Additional information

Original Russian Text © V.S. Moiseeva, T.N. Murugova, I.M. Vangeli, I.M. Byvshev, S. Ravaud, R.A. Simonyan, V.I. Gordeliy, E. Pebay-Peyroula, L.S. Yaguzhinsky, 2017, published in Biologicheskie Membrany, 2017, Vol. 34, No. 6, pp. 155–163.

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Moiseeva, V.S., Murugova, T.N., Vangeli, I.M. et al. On the mechanism and functional significance of the ADP/ATP carrier (AAC) dimerization. Biochem. Moscow Suppl. Ser. A 11, 321–329 (2017). https://doi.org/10.1134/S1990747817040079

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  • DOI: https://doi.org/10.1134/S1990747817040079

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