Enviar artigo por via de e-mail On the mechanism and functional significance of the ADP/ATP carrier (AAC) dimerization
- Autores: Moiseeva V.1, Murugova T.2,3, Vangeli I.4, Byvshev I.3, Ravaud S.1, Simonyan R.4, Gordeliy V.1,3,5, Pebay-Peyroula E.1, Yaguzhinsky L.3,4
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Afiliações:
- Institut de Biologie Structurale (IBS), University Grenoble Alpes, CEA
- Frank Laboratory of Neutron Physics
- Moscow Institute of Physics and Technology
- Belozersky Institute of Physico-Chemical Biology
- Institute of Complex Systems (ICS), ICS-6: Structural Biochemistry
- Edição: Volume 11, Nº 4 (2017)
- Páginas: 321-329
- Seção: Articles
- URL: https://journals.rcsi.science/1990-7478/article/view/213277
- DOI: https://doi.org/10.1134/S1990747817040079
- ID: 213277
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Resumo
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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Sobre autores
V. Moiseeva
Institut de Biologie Structurale (IBS), University Grenoble Alpes, CEA
Email: yag@genebee.msu.su
França, Grenoble, 38044
T. Murugova
Frank Laboratory of Neutron Physics; Moscow Institute of Physics and Technology
Email: yag@genebee.msu.su
Rússia, Dubna, 141980; Dolgoprudny, 141701
I. Vangeli
Belozersky Institute of Physico-Chemical Biology
Email: yag@genebee.msu.su
Rússia, Moscow, 119992
I. Byvshev
Moscow Institute of Physics and Technology
Email: yag@genebee.msu.su
Rússia, Dolgoprudny, 141701
S. Ravaud
Institut de Biologie Structurale (IBS), University Grenoble Alpes, CEA
Email: yag@genebee.msu.su
França, Grenoble, 38044
R. Simonyan
Belozersky Institute of Physico-Chemical Biology
Email: yag@genebee.msu.su
Rússia, Moscow, 119992
V. Gordeliy
Institut de Biologie Structurale (IBS), University Grenoble Alpes, CEA; Moscow Institute of Physics and Technology; Institute of Complex Systems (ICS), ICS-6: Structural Biochemistry
Email: yag@genebee.msu.su
França, Grenoble, 38044; Dolgoprudny, 141701; Juelich, 52425
E. Pebay-Peyroula
Institut de Biologie Structurale (IBS), University Grenoble Alpes, CEA
Email: yag@genebee.msu.su
França, Grenoble, 38044
L. Yaguzhinsky
Moscow Institute of Physics and Technology; Belozersky Institute of Physico-Chemical Biology
Autor responsável pela correspondência
Email: yag@genebee.msu.su
Rússia, Dolgoprudny, 141701; Moscow, 119992
