title: The role of tubulin in the mitochondrial metabolism and arrangement in muscle cells.
abstract: Tubulin, a well-known component of the microtubule in the cytoskeleton, has an important role in the transport and positioning of mitochondria in a cell type dependent manner. This review describes different functional interactions of tubulin with cellular protein complexes and its functional interaction with the mitochondrial outer membrane. Tubulin is present in oxidative as well as glycolytic type muscle cells, but the kinetics of the in vivo regulation of mitochondrial respiration in these muscle types is drastically different. The interaction between VDAC and tubulin is probably influenced by such factors as isoformic patterns of VDAC and tubulin, post-translational modifications of tubulin and phosphorylation of VDAC. Important factor of the selective permeability of VDAC is the mitochondrial creatine kinase pathway which is present in oxidative cells, but is inactive or missing in glycolytic muscle and cancer cells. As the tubulin-VDAC interaction reduces the permeability of the channel by adenine nucleotides, energy transfer can then take place effectively only through the mitochondrial creatine kinase/phosphocreatine pathway. Therefore, closure of VDAC by tubulin may be one of the reasons of apoptosis in cells without the creatine kinase pathway. An important question in tubulin regulated interactions is whether other proteins are interacting with tubulin. The functional interaction may be direct, through other proteins like plectins, or influenced by simultaneous interaction of other complexes with VDAC.
authors.affiliation: Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, Tallinn, 12618, Estonia, kersti.tepp@kbfi.ee.
authors.forename: Kersti
authors.initials: K
authors.lastname: Tepp
authors.forename: Kati
authors.initials: K
authors.lastname: Mado
authors.forename: Minna
authors.initials: M
authors.lastname: Varikmaa
authors.forename: Aleksandr
authors.initials: A
authors.lastname: Klepinin
authors.forename: Natalja
authors.initials: N
authors.lastname: Timohhina
authors.forename: Igor
authors.initials: I
authors.lastname: Shevchuk
authors.forename: Vladimir
authors.initials: V
authors.lastname: Chekulayev
authors.forename: Andrey V
authors.initials: AV
authors.lastname: Kuznetsov
authors.forename: Rita
authors.initials: R
authors.lastname: Guzun
authors.forename: Tuuli
authors.initials: T
authors.lastname: Kaambre
mesh_terms: D000818:Animals; D003599:Cytoskeleton / Q000378:metabolism; D006801:Humans; D008931:Mitochondria, Muscle / Q000378:metabolism*; D051336:Mitochondrial Membranes / Q000378:metabolism*; D011485:Protein Binding; D014404:Tubulin / Q000378:metabolism*; D050994:Voltage-Dependent Anion Channels / Q000378:metabolism
chemical_list: D014404:Tubulin; D050994:Voltage-Dependent Anion Channels