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Puurand 2019 Cells

From Bioblast
Publications in the MiPMap
Puurand M, Tepp K, Timohhina N, Aid J, Shevchuk I, Chekulayev V, Kaambre T (2019) Tubulin βII and βIII isoforms as the regulators of VDAC channel permeability in health and disease. Cells 8:E239.

» PMID:30871176 Open Access

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 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. Keywords: Brain, Cancer, Creatine kinase, Hexokinase, Mitochondria, Oxidative muscle, Oxidative phosphorylation, Synaptosomes, Tubulin, Voltage-dependent anion channel (VDAC) Bioblast editor: Plangger M O2k-Network Lab: EE Tallinn Kaambre T

Labels: MiParea: Respiration, mt-Membrane 

Regulation: Ion;substrate transport 

HRR: Oxygraph-2k 

Labels, 2019-03