Puurand 2019 Cells
| Puurand M, Tepp K, Timohhina N, Aid J, Shevchuk I, Chekulayev V, Kaambre T (2019) Tubulin Ξ²II and Ξ²III isoforms as the regulators of VDAC channel permeability in health and disease. Cells 8:E239. |
Puurand M, Tepp K, Timohhina N, Aid J, Shevchuk I, Chekulayev V, Kaambre T (2019) Cells
Abstract: 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 Ξ²-tubulin, bound to VDAC. It is also thought that Ξ²-tubulinβVDAC 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 Ξ±Ξ²-tubulin heterodimers in regulating VDAC permeability for adenine nucleotides and cellular bioenergetics. We introduce the Mitochondrial Interactosome model and the function of the Ξ²II-tubulin subunit in this model in muscle cells and brain synaptosomes, and also consider the role of Ξ²III-tubulin in cancer cells. β’ Keywords: Brain, Cancer, Creatine kinase, Hexokinase, Mitochondria, Oxidative muscle, Oxidative phosphorylation, Synaptosomes, Tubulin, Voltage-dependent anion channel (VDAC) β’ Bioblast editor: Plangger M β’ O2k-Network Lab: EE Tallinn Kaambre T
Labels: MiParea: Respiration, mt-Membrane
Regulation: Ion;substrate transport
HRR: Oxygraph-2k
Labels, 2019-03
