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Tubulin βII and βIII Isoforms as the Regulators of VDAC Channel Permeability in Health and Disease

Laboratory of Chemical Biology, National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, 12618 Tallinn, Estonia
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Cells 2019, 8(3), 239; https://doi.org/10.3390/cells8030239
Received: 28 January 2019 / Revised: 7 March 2019 / Accepted: 9 March 2019 / Published: 13 March 2019
(This article belongs to the Special Issue Tubulin: Structure, Functions and Roles in Disease)
In recent decades, there have been several models describing the relationships between the cytoskeleton and the bioenergetic function of the cell. The main player in these models is the voltage-dependent anion channel (VDAC), located in the mitochondrial outer membrane. Most metabolites including respiratory substrates, ADP, and Pi enter mitochondria only through VDAC. At the same time, high-energy phosphates are channeled out and directed to cellular energy transfer networks. Regulation of these energy fluxes is controlled by β-tubulin, bound to VDAC. It is also thought that β-tubulin‒VDAC interaction modulates cellular energy metabolism in cancer, e.g., switching from oxidative phosphorylation to glycolysis. In this review we focus on the described roles of unpolymerized αβ-tubulin heterodimers in regulating VDAC permeability for adenine nucleotides and cellular bioenergetics. We introduce the Mitochondrial Interactosome model and the function of the βII-tubulin subunit in this model in muscle cells and brain synaptosomes, and also consider the role of βIII-tubulin in cancer cells. View Full-Text
Keywords: tubulin; voltage-dependent anion channel (VDAC); mitochondria; hexokinase; oxidative phosphorylation; creatine kinase; oxidative muscle; brain; synaptosomes; cancer tubulin; voltage-dependent anion channel (VDAC); mitochondria; hexokinase; oxidative phosphorylation; creatine kinase; oxidative muscle; brain; synaptosomes; cancer
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MDPI and ACS Style

Puurand, M.; Tepp, K.; Timohhina, N.; Aid, J.; Shevchuk, I.; Chekulayev, V.; Kaambre, T. Tubulin βII and βIII Isoforms as the Regulators of VDAC Channel Permeability in Health and Disease. Cells 2019, 8, 239. https://doi.org/10.3390/cells8030239

AMA Style

Puurand M, Tepp K, Timohhina N, Aid J, Shevchuk I, Chekulayev V, Kaambre T. Tubulin βII and βIII Isoforms as the Regulators of VDAC Channel Permeability in Health and Disease. Cells. 2019; 8(3):239. https://doi.org/10.3390/cells8030239

Chicago/Turabian Style

Puurand, Marju; Tepp, Kersti; Timohhina, Natalja; Aid, Jekaterina; Shevchuk, Igor; Chekulayev, Vladimir; Kaambre, Tuuli. 2019. "Tubulin βII and βIII Isoforms as the Regulators of VDAC Channel Permeability in Health and Disease" Cells 8, no. 3: 239. https://doi.org/10.3390/cells8030239

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