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Journal articles on the topic 'Tubulin'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Shu, H. B., and H. C. Joshi. "Gamma-tubulin can both nucleate microtubule assembly and self-assemble into novel tubular structures in mammalian cells." Journal of Cell Biology 130, no. 5 (1995): 1137–47. http://dx.doi.org/10.1083/jcb.130.5.1137.

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alpha-, beta-, and gamma-tubulins are evolutionarily highly conserved members of the tubulin gene superfamily. While the abundant members, alpha- and beta-tubulins, constitute the building blocks of cellular microtubule polymers, gamma-tubulin is a low abundance protein which localized to the pericentriolar material and may play a role in microtubule assembly. To test whether gamma-tubulin mediates the nucleation of microtubule assembly in vivo, and co-assembles with alpha- and beta-tubulins into microtubules or self-assembles into macro-molecular structures, we experimentally elevated the exp

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2

Inclan, Y. F., and E. Nogales. "Structural models for the self-assembly and microtubule interactions of gamma-, delta- and epsilon-tubulin." Journal of Cell Science 114, no. 2 (2001): 413–22. http://dx.doi.org/10.1242/jcs.114.2.413.

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alphabeta-tubulin heterodimers self-assemble to form microtubules nucleated by gamma-tubulin in the cell. Gamma-tubulin is believed to recruit the alphabeta-tubulin dimers that form the minus ends of microtubules, but the molecular mechanism of this action remains a matter of heated controversy. Still less is known about the function and molecular interactions of delta-tubulin and epsilon-tubulin. delta-tubulin may seed the formation of the C triplet tubules in the basal bodies of Chlamydomonas and epsilon-tubulin is known to localize to the centrosome in a cell cycle-dependent manner. Using t

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3

Burke, D., P. Gasdaska, and L. Hartwell. "Dominant effects of tubulin overexpression in Saccharomyces cerevisiae." Molecular and Cellular Biology 9, no. 3 (1989): 1049–59. http://dx.doi.org/10.1128/mcb.9.3.1049-1059.1989.

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The consequences of altering the levels of alpha- and beta-tubulin in Saccharomyces cerevisiae were examined by constructing fusions of the structural genes encoding the tubulins to strong galactose-inducible promoters. Overexpression of beta-tubulin (TUB2) was lethal: cells arrested in the G2 stage of the cell cycle exhibited an increased frequency of chromosome loss, were devoid of microtubules, and accumulated beta-tubulin in a novel structure. Overexpression of the major alpha-tubulin gene (TUB1) was not lethal and did not affect chromosome segregation. The rate of alpha-tubulin mRNA and p

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4

Burke, D., P. Gasdaska, and L. Hartwell. "Dominant effects of tubulin overexpression in Saccharomyces cerevisiae." Molecular and Cellular Biology 9, no. 3 (1989): 1049–59. http://dx.doi.org/10.1128/mcb.9.3.1049.

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The consequences of altering the levels of alpha- and beta-tubulin in Saccharomyces cerevisiae were examined by constructing fusions of the structural genes encoding the tubulins to strong galactose-inducible promoters. Overexpression of beta-tubulin (TUB2) was lethal: cells arrested in the G2 stage of the cell cycle exhibited an increased frequency of chromosome loss, were devoid of microtubules, and accumulated beta-tubulin in a novel structure. Overexpression of the major alpha-tubulin gene (TUB1) was not lethal and did not affect chromosome segregation. The rate of alpha-tubulin mRNA and p

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5

Burland, T. G., E. C. Paul, M. Oetliker, and W. F. Dove. "A gene encoding the major beta tubulin of the mitotic spindle in Physarum polycephalum plasmodia." Molecular and Cellular Biology 8, no. 3 (1988): 1275–81. http://dx.doi.org/10.1128/mcb.8.3.1275-1281.1988.

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The multinucleate plasmodium of Physarum polycephalum is unusual among eucaryotic cells in that it uses tubulins only in mitotic-spindle microtubules; cytoskeletal, flagellar, and centriolar microtubules are absent in this cell type. We have identified a beta-tubulin cDNA clone, beta 105, which is shown to correspond to the transcript of the betC beta-tubulin locus and to encode beta 2 tubulin, the beta tubulin expressed specifically in the plasmodium and used exclusively in the mitotic spindle. Physarum amoebae utilize tubulins in the cytoskeleton, centrioles, and flagella, in addition to the

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6

Burland, T. G., E. C. Paul, M. Oetliker, and W. F. Dove. "A gene encoding the major beta tubulin of the mitotic spindle in Physarum polycephalum plasmodia." Molecular and Cellular Biology 8, no. 3 (1988): 1275–81. http://dx.doi.org/10.1128/mcb.8.3.1275.

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The multinucleate plasmodium of Physarum polycephalum is unusual among eucaryotic cells in that it uses tubulins only in mitotic-spindle microtubules; cytoskeletal, flagellar, and centriolar microtubules are absent in this cell type. We have identified a beta-tubulin cDNA clone, beta 105, which is shown to correspond to the transcript of the betC beta-tubulin locus and to encode beta 2 tubulin, the beta tubulin expressed specifically in the plasmodium and used exclusively in the mitotic spindle. Physarum amoebae utilize tubulins in the cytoskeleton, centrioles, and flagella, in addition to the

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7

Zhou, Yujun, Jianqiang Xu, Yuanye Zhu, Yabing Duan, and Mingguo Zhou. "Mechanism of Action of the Benzimidazole Fungicide on Fusarium graminearum: Interfering with Polymerization of Monomeric Tubulin But Not Polymerized Microtubule." Phytopathology® 106, no. 8 (2016): 807–13. http://dx.doi.org/10.1094/phyto-08-15-0186-r.

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Tubulins are the proposed target of clinically relevant anticancer drugs, anthelmintic, and fungicide. β2-tubulin of the plant pathogen Fusarium graminearum was considered as the target of benzimidazole compounds by homology modeling in our previous work. In this study, α1-, α2-, and β2-tubulin of F. graminearum were produced in Escherichia coli. Three benzimidazole compounds (carbendazim, benomyl, and thiabendazole) interacted with the recombinant β2-tubulin and reduced the maximum fluorescence intensity of 2 μM β2-tubulin 47, 50, and 25%, respectively, at saturation of compound-tubulin compl

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8

Rudolph, J. E., M. Kimble, H. D. Hoyle, M. A. Subler, and E. C. Raff. "Three Drosophila beta-tubulin sequences: a developmentally regulated isoform (beta 3), the testis-specific isoform (beta 2), and an assembly-defective mutation of the testis-specific isoform (B2t8) reveal both an ancient divergence in metazoan isotypes and structural constraints for beta-tubulin function." Molecular and Cellular Biology 7, no. 6 (1987): 2231–42. http://dx.doi.org/10.1128/mcb.7.6.2231-2242.1987.

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The genomic DNA sequence and deduced amino acid sequence are presented for three Drosophila melanogaster beta-tubulins: a developmentally regulated isoform beta 3-tubulin, the wild-type testis-specific isoform beta 2-tubulin, and an ethyl methanesulfonate-induced assembly-defective mutation of the testis isoform, B2t8. The testis-specific beta 2-tubulin is highly homologous to the major vertebrate beta-tubulins, but beta 3-tubulin is considerably diverged. Comparison of the amino acid sequences of the two Drosophila isoforms to those of other beta-tubulins indicates that these two proteins are

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9

Rudolph, J. E., M. Kimble, H. D. Hoyle, M. A. Subler, and E. C. Raff. "Three Drosophila beta-tubulin sequences: a developmentally regulated isoform (beta 3), the testis-specific isoform (beta 2), and an assembly-defective mutation of the testis-specific isoform (B2t8) reveal both an ancient divergence in metazoan isotypes and structural constraints for beta-tubulin function." Molecular and Cellular Biology 7, no. 6 (1987): 2231–42. http://dx.doi.org/10.1128/mcb.7.6.2231.

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The genomic DNA sequence and deduced amino acid sequence are presented for three Drosophila melanogaster beta-tubulins: a developmentally regulated isoform beta 3-tubulin, the wild-type testis-specific isoform beta 2-tubulin, and an ethyl methanesulfonate-induced assembly-defective mutation of the testis isoform, B2t8. The testis-specific beta 2-tubulin is highly homologous to the major vertebrate beta-tubulins, but beta 3-tubulin is considerably diverged. Comparison of the amino acid sequences of the two Drosophila isoforms to those of other beta-tubulins indicates that these two proteins are

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10

Chu, Chih-Wen, Fajian Hou, Junmei Zhang та ін. "A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation". Molecular Biology of the Cell 22, № 4 (2011): 448–56. http://dx.doi.org/10.1091/mbc.e10-03-0203.

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Dynamic instability is a critical property of microtubules (MTs). By regulating the rate of tubulin polymerization and depolymerization, cells organize the MT cytoskeleton to accommodate their specific functions. Among many processes, posttranslational modifications of tubulin are implicated in regulating MT functions. Here we report a novel tubulin acetylation catalyzed by acetyltransferase San at lysine 252 (K252) of β-tubulin. This acetylation, which is also detected in vivo, is added to soluble tubulin heterodimers but not tubulins in MTs. The acetylation-mimicking K252A/Q mutants were inc

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11

Schneider, A., U. Plessmann, and K. Weber. "Subpellicular and flagellar microtubules of Trypanosoma brucei are extensively glutamylated." Journal of Cell Science 110, no. 4 (1997): 431–37. http://dx.doi.org/10.1242/jcs.110.4.431.

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To determine the spectrum of tubulin variants in cytoskeletons of Trypanosoma brucei carboxy-terminal fragments of alpha- and beta-tubulin were isolated and characterized by sequencing and mass spectrometry. All variants arise by posttranslational modifications. We confirm the presence of tyrosinated and detyrosinated alpha-tubulin. Unexpectedly, but in line with its sequence, beta-tubulin also occurs with and without its carboxy-terminal tyrosine. Both tyrosinated and detyrosinated alpha- and beta-tubulins are extensively glutamylated. Unglutamylated tubulins are only trace components of the

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12

Chumová, Jana, Hana Kourová, Lucie Trögelová, Petr Halada та Pavla Binarová. "Microtubular and Nuclear Functions of γ-Tubulin: Are They LINCed?" Cells 8, № 3 (2019): 259. http://dx.doi.org/10.3390/cells8030259.

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γ-Tubulin is a conserved member of the tubulin superfamily with a function in microtubule nucleation. Proteins of γ-tubulin complexes serve as nucleation templates as well as a majority of other proteins contributing to centrosomal and non-centrosomal nucleation, conserved across eukaryotes. There is a growing amount of evidence of γ-tubulin functions besides microtubule nucleation in transcription, DNA damage response, chromatin remodeling, and on its interactions with tumor suppressors. However, the molecular mechanisms are not well understood. Furthermore, interactions with lamin and SUN pr

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13

Yu, Nuo, and Niels Galjart. "TAPping into the treasures of tubulin using novel protein production methods." Essays in Biochemistry 62, no. 6 (2018): 781–92. http://dx.doi.org/10.1042/ebc20180033.

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Microtubules are cytoskeletal elements with important cellular functions, whose dynamic behaviour and properties are in part regulated by microtubule-associated proteins (MAPs). The building block of microtubules is tubulin, a heterodimer of α- and β-tubulin subunits. Longitudinal interactions between tubulin dimers facilitate a head-to-tail arrangement of dimers into protofilaments, while lateral interactions allow the formation of a hollow microtubule tube that mostly contains 13 protofilaments. Highly homologous α- and β-tubulin isotypes exist, which are encoded by multi-gene families. In v

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14

SULIMENKO, Vadym, Tetyana SULIMENKO, Slobodan POZNANOVIC та ін. "Association of brain γ-tubulins with αβ-tubulin dimers". Biochemical Journal 365, № 3 (2002): 889–95. http://dx.doi.org/10.1042/bj20020175.

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γ-Tubulin is necessary for nucleation and polar orientation of microtubules in vivo. The molecular mechanism of microtubule nucleation by γ-tubulin and the regulation of this process are not fully understood. Here we show that there are two γ-tubulin forms in the brain that are present in complexes of various sizes. Large complexes tend to dissociate in the presence of a high salt concentration. Both γ-tubulins co-polymerized with tubulin dimers, and multiple γ-tubulin bands were identified in microtubule protein preparations under conditions of non-denaturing electrophoresis. Immunoprecipitat

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15

Hoyle, H. D., and E. C. Raff. "Two Drosophila beta tubulin isoforms are not functionally equivalent." Journal of Cell Biology 111, no. 3 (1990): 1009–26. http://dx.doi.org/10.1083/jcb.111.3.1009.

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We have tested the functional capacity of different beta tubulin isoforms in vivo by expressing beta 3-tubulin either in place of or in addition to beta 2-tubulin in the male germ line of Drosophila melanogaster. The testes-specific isoform, beta 2, is conserved relative to major metazoan beta tubulins, while the developmentally regulated isoform, beta 3, is considerably divergent in sequence. beta 3-tubulin is normally expressed in discrete subsets of cells at specific times during development, but is not expressed in the male germ line. beta 2-Tubulin is normally expressed only in the postmi

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16

Lin, Zhewang, Ivana Gasic, Viswanathan Chandrasekaran, et al. "TTC5 mediates autoregulation of tubulin via mRNA degradation." Science 367, no. 6473 (2019): 100–104. http://dx.doi.org/10.1126/science.aaz4352.

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Tubulins play crucial roles in cell division, intracellular traffic, and cell shape. Tubulin concentration is autoregulated by feedback control of messenger RNA (mRNA) degradation via an unknown mechanism. We identified tetratricopeptide protein 5 (TTC5) as a tubulin-specific ribosome-associating factor that triggers cotranslational degradation of tubulin mRNAs in response to excess soluble tubulin. Structural analysis revealed that TTC5 binds near the ribosome exit tunnel and engages the amino terminus of nascent tubulins. TTC5 mutants incapable of ribosome or nascent tubulin interaction abol

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17

Pamula, Melissa C., Shih-Chieh Ti та Tarun M. Kapoor. "The structured core of human β tubulin confers isotype-specific polymerization properties". Journal of Cell Biology 213, № 4 (2016): 425–33. http://dx.doi.org/10.1083/jcb.201603050.

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Diversity in cytoskeleton organization and function may be achieved through variations in primary sequence of tubulin isotypes. Recently, isotype functional diversity has been linked to a “tubulin code” in which the C-terminal tail, a region of substantial sequence divergence between isotypes, specifies interactions with microtubule-associated proteins. However, it is not known whether residue changes in this region alter microtubule dynamic instability. Here, we examine recombinant tubulin with human β isotype IIB and characterize polymerization dynamics. Microtubules with βIIB have catastrop

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18

Liu, Congshan, Jiaqing Yao, Jianhai Yin, Jian Xue та Haobing Zhang. "Recombinant α- and β-tubulin from Echinococcus granulosus: expression, purification and polymerization". Parasite 25 (2018): 62. http://dx.doi.org/10.1051/parasite/2018063.

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Echinococcosis, which causes a high disease burden and is of great public health significance, is caused by the larval stage of Echinococcus species. It has been suggested that tubulin is the target of benzimidazoles, the only drugs for the treatment of echinococcosis. This study evaluated the characteristics of tubulins from Echinococcus granulosus. The full-length cDNAs of E. granulosus α- and β-tubulin isoforms were cloned by reverse transcription PCR from protoscolex RNA. Then, these two tubulin isoforms (α9 and β4) were recombinantly expressed as insoluble inclusion bodies in Escherichia

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19

Trivinos-Lagos, L., T. Ohmachi, C. Albrightson, R. G. Burns, H. L. Ennis, and R. L. Chisholm. "The highly divergent alpha- and beta-tubulins from Dictyostelium discoideum are encoded by single genes." Journal of Cell Science 105, no. 4 (1993): 903–11. http://dx.doi.org/10.1242/jcs.105.4.903.

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As a step in the characterization of the microtubule system of Dictyostelium discoideum, we have isolated and sequenced full-length cDNA clones that encode the Dictyostelium alpha- and beta-tubulins, as well as the Dictyostelium alpha-tubulin gene. Southern blot analysis suggests that Dictyostelium is unusual in that its genome contains single alpha- and beta-tubulin genes, rather than the multi-gene family common in most eukaryotic organisms. The complete alpha-tubulin cDNA contains 1558 nucleotides, with an open reading frame, that encode a protein of 457 amino acids. The complete beta-tubul

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20

Kristensson, Maria Alvarado. "The Game of Tubulins." Cells 10, no. 4 (2021): 745. http://dx.doi.org/10.3390/cells10040745.

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Members of the tubulin superfamily are GTPases; the activities of GTPases are necessary for life. The members of the tubulin superfamily are the constituents of the microtubules and the γ-tubulin meshwork. Mutations in members of the tubulin superfamily are involved in developmental brain disorders, and tubulin activities are the target for various chemotherapies. The intricate functions (game) of tubulins depend on the activities of the GTP-binding domain of α-, β-, and γ-tubulin. This review compares the GTP-binding domains of γ-tubulin, α-tubulin, and β-tubulin and, based on their similarit

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21

Gong, Z. Y., and B. P. Brandhorst. "Stimulation of tubulin gene transcription by deciliation of sea urchin embryos." Molecular and Cellular Biology 7, no. 12 (1987): 4238–46. http://dx.doi.org/10.1128/mcb.7.12.4238-4246.1987.

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Deciliation by hypertonic shock of embryos of the sea urchin Lytechinus pictus resulted in an increase in synthesis of alpha- and beta-tubulins, the consequence of an increased concentration of RNA encoding the tubulins. RNA run-on assays in isolated nuclei indicated that this response is due to a transient increase in the rate of synthesis of tubulin RNA beginning within 5 min of deciliation. This enhancement of tubulin gene transcription also occurred in deciliated embryos treated with the microtubule-depolymerizing agent colcemid; thus the reaction to deciliation is not a response to a redu

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22

Gong, Z. Y., and B. P. Brandhorst. "Stimulation of tubulin gene transcription by deciliation of sea urchin embryos." Molecular and Cellular Biology 7, no. 12 (1987): 4238–46. http://dx.doi.org/10.1128/mcb.7.12.4238.

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Deciliation by hypertonic shock of embryos of the sea urchin Lytechinus pictus resulted in an increase in synthesis of alpha- and beta-tubulins, the consequence of an increased concentration of RNA encoding the tubulins. RNA run-on assays in isolated nuclei indicated that this response is due to a transient increase in the rate of synthesis of tubulin RNA beginning within 5 min of deciliation. This enhancement of tubulin gene transcription also occurred in deciliated embryos treated with the microtubule-depolymerizing agent colcemid; thus the reaction to deciliation is not a response to a redu

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23

Al-Bassam, Jawdat. "Revisiting the tubulin cofactors and Arl2 in the regulation of soluble αβ-tubulin pools and their effect on microtubule dynamics". Molecular Biology of the Cell 28, № 3 (2017): 359–63. http://dx.doi.org/10.1091/mbc.e15-10-0694.

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Soluble αβ-tubulin heterodimers are maintained at high concentration inside eukaryotic cells, forming pools that fundamentally drive microtubule dynamics. Five conserved tubulin cofactors and ADP ribosylation factor–like 2 regulate the biogenesis and degradation of αβ-tubulins to maintain concentrated soluble pools. Here I describe a revised model for the function of three tubulin cofactors and Arl2 as a multisubunit GTP-hydrolyzing catalytic chaperone that cycles to promote αβ-tubulin biogenesis and degradation. This model helps explain old and new data indicating these activities enhance mic

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24

Weatherbee, J. A., G. S. May, J. Gambino, and N. R. Morris. "Involvement of a particular species of beta-tubulin (beta 3) in conidial development in Aspergillus nidulans." Journal of Cell Biology 101, no. 3 (1985): 706–11. http://dx.doi.org/10.1083/jcb.101.3.706.

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Strains of Aspergillus containing the benA22 mutation are resistant to benomyl for vegetative growth but do not produce conidia. To test whether conidiation involved an additional benomyl-sensitive tubulin (i.e., was mediated by a tubulin other than the tubulins coded for by the benA locus), a collection of mutants was produced that formed conidia in the presence of benomyl, i.e., were conidiation-resistant (CR-) mutants. We analyzed the tubulins of these CR- mutants using two-dimensional gel electrophoresis and found that the mutants lacked one species of beta-tubulin (designated beta 3). We

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25

Saoudi, Y., I. Paintrand, L. Multigner, and D. Job. "Stabilization and bundling of subtilisin-treated microtubules induced by microtubule associated proteins." Journal of Cell Science 108, no. 1 (1995): 357–67. http://dx.doi.org/10.1242/jcs.108.1.357.

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The acidic carboxy-terminal regions of alpha- and beta-tubulin subunits are currently thought to be centrally involved in microtubule stability and in microtubule association with a variety of proteins (MAPs) such as MAP2 and tau proteins. Here, pure tubulin microtubules were exposed to subtilisin to produce polymers composed of cleaved tubulin subunits lacking carboxy termini. Polymer exposure to subtilisin was achieved in buffer conditions compatible with further tests of microtubule stability. Microtubules composed of normal alpha-tubulin and cleaved beta-tubulin were indistinguishable from

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26

Xie, Yixin, and Lin Li. "Computational Study on E-Hooks of Tubulins in the Binding Process with Kinesin." International Journal of Molecular Sciences 23, no. 4 (2022): 2035. http://dx.doi.org/10.3390/ijms23042035.

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Cargo transport within cells is essential to healthy cells, which requires microtubules-based motors, including kinesin. The C-terminal tails (E-hooks) of alpha and beta tubulins of microtubules have been proven to play important roles in interactions between the kinesins and tubulins. Here, we implemented multi-scale computational methods in E-hook-related analyses, including flexibility investigations of E-hooks, binding force calculations at binding interfaces between kinesin and tubulins, electrostatic potential calculations on the surface of kinesin and tubulins. Our results show that E-h

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27

Khabudaev, Kirill V., Darya P. Petrova, Yekaterina D. Bedoshvili, Yelena V. Likhoshway, and Mikhail A. Grachev. "Molecular Evolution of Tubulins in Diatoms." International Journal of Molecular Sciences 23, no. 2 (2022): 618. http://dx.doi.org/10.3390/ijms23020618.

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Microtubules are formed by α- and β-tubulin heterodimers nucleated with γ-tubulin. Tubulins are conserved eukaryotic proteins. Previously, it was shown that microtubules are involved in diatom silica frustule morphogenesis. Diatom frustules are varied, and their morphology is species-specific. Despite the attractiveness of the problem of elucidating the molecular mechanisms of genetically programmed morphogenesis, the structure and evolution of diatom tubulins have not been studied previously. Based on available genomic and transcriptome data, we analyzed the phylogeny of the predicted amino a

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Hoyle, Henry D., F. Rudolf Turner, Linda Brunick, and Elizabeth C. Raff. "Tubulin Sorting during Dimerization In Vivo." Molecular Biology of the Cell 12, no. 7 (2001): 2185–94. http://dx.doi.org/10.1091/mbc.12.7.2185.

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We demonstrate sorting of β-tubulins during dimerization in theDrosophila male germ line. Different β-tubulin isoforms exhibit distinct affinities for α-tubulin during dimerization. Our data suggest that differences in dimerization properties are important in determining isoform-specific microtubule functions. The differential use of β-tubulin during dimerization reveals structural parameters of the tubulin heterodimer not discernible in the resolved three-dimensional structure. We show that the variable β-tubulin carboxyl terminus, a surface feature in the heterodimer and in microtubules, and

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Lajoie-Mazenc, I., C. Detraves, V. Rotaru, et al. "A single gamma-tubulin gene and mRNA, but two gamma-tubulin polypeptides differing by their binding to the spindle pole organizing centres." Journal of Cell Science 109, no. 10 (1996): 2483–92. http://dx.doi.org/10.1242/jcs.109.10.2483.

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Cells of eukaryotic organisms exhibit microtubules with various functions during the different developmental stages. The identification of multiple forms of alpha- and beta-tubulins had raised the question of their possible physiological roles. In the myxomycete Physarum polycephalum a complex polymorphism for alpha- and beta-tubulins has been correlated with a specific developmental expression pattern. Here, we have investigated the potential heterogeneity of gamma-tubulin in this organism. A single gene, with 3 introns and 4 exons, and a single mRNA coding for gamma-tubulin were detected. Th

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Guo, Wenhan, Tolulope Ayodeji Ale, Shengjie Sun, Jason E. Sanchez, and Lin Li. "A Comprehensive Study on the Electrostatic Properties of Tubulin-Tubulin Complexes in Microtubules." Cells 12, no. 2 (2023): 238. http://dx.doi.org/10.3390/cells12020238.

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Microtubules are key players in several stages of the cell cycle and are also involved in the transportation of cellular organelles. Microtubules are polymerized by α/β tubulin dimers with a highly dynamic feature, especially at the plus ends of the microtubules. Therefore, understanding the interactions among tubulins is crucial for characterizing microtubule dynamics. Studying microtubule dynamics can help researchers make advances in the treatment of neurodegenerative diseases and cancer. In this study, we utilize a series of computational approaches to study the electrostatic interactions

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Johnson, K. A. "The axonemal microtubules of the Chlamydomonas flagellum differ in tubulin isoform content." Journal of Cell Science 111, no. 3 (1998): 313–20. http://dx.doi.org/10.1242/jcs.111.3.313.

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Little is known of the molecular basis for the diversity of microtubule structure and function found within the eukaryotic flagellum. Antibodies that discriminate between tyrosinated alpha tubulin and post-translationally detyrosinated alpha tubulin were used to localize these complementary tubulin isoforms in flagella of the single-celled green alga Chlamydomonas reinhardtii. Immunofluorescence analysis of intact axonemes detected both isoforms along most of the lengths of flagella; however, each had a short distal zone rich in tyrosinated tubulin. Localizations on splayed axonemes revealed t

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32

Hecht, N. B., R. J. Distel, P. C. Yelick, et al. "Localization of a highly divergent mammalian testicular alpha tubulin that is not detectable in brain." Molecular and Cellular Biology 8, no. 2 (1988): 996–1000. http://dx.doi.org/10.1128/mcb.8.2.996-1000.1988.

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Sequence analysis of a mouse testicular alpha-tubulin partial cDNA, pRD alpha TT1, reveals an isotype that differs from both the somatic and the predominant testicular alpha tubulins at approximately 30% of the 212 amino acid residues determined. Although this mouse testicular cDNA retains the highly conserved sequence, Glu-Gly-Glu-Glu, found in the carboxyl termini of many alpha tubulins, the protein extends substantially beyond this sequence and does not terminate with a C-terminal tyrosine. Using rabbit antiserum prepared to a novel synthetic peptide predicted from this mouse testis alpha-t

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33

Hecht, N. B., R. J. Distel, P. C. Yelick, et al. "Localization of a highly divergent mammalian testicular alpha tubulin that is not detectable in brain." Molecular and Cellular Biology 8, no. 2 (1988): 996–1000. http://dx.doi.org/10.1128/mcb.8.2.996.

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Sequence analysis of a mouse testicular alpha-tubulin partial cDNA, pRD alpha TT1, reveals an isotype that differs from both the somatic and the predominant testicular alpha tubulins at approximately 30% of the 212 amino acid residues determined. Although this mouse testicular cDNA retains the highly conserved sequence, Glu-Gly-Glu-Glu, found in the carboxyl termini of many alpha tubulins, the protein extends substantially beyond this sequence and does not terminate with a C-terminal tyrosine. Using rabbit antiserum prepared to a novel synthetic peptide predicted from this mouse testis alpha-t

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Ruiz, F., P. Dupuis-Williams, C. Klotz та ін. "Genetic Evidence for Interaction between η- and β-Tubulins". Eukaryotic Cell 3, № 1 (2004): 212–20. http://dx.doi.org/10.1128/ec.3.1.212-220.2004.

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ABSTRACT The thermosensitive allelic mutations sm19-1 and sm19-2 of Paramecium tetraurelia cause defective basal body duplication: growth at the nonpermissive temperature yields smaller and smaller cells with fewer and fewer basal bodies. Complementation cloning of the SM19 gene identified a new tubulin, eta-tubulin, showing low homology with each of the other five tubulins, α to ε, characterized in P. tetraurelia. In order to analyze η-tubulin functions, we used a genetic approach to identify interacting molecules. Among a series of extragenic suppressors of the sm19-1 mutation, the su3-1 mut

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Nami, Babak, and Zhixiang Wang. "Genetics and Expression Profile of the Tubulin Gene Superfamily in Breast Cancer Subtypes and Its Relation to Taxane Resistance." Cancers 10, no. 8 (2018): 274. http://dx.doi.org/10.3390/cancers10080274.

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Taxanes are a class of chemotherapeutic agents that inhibit cell division by disrupting the mitotic spindle through the stabilization of microtubules. Most breast cancer (BC) tumors show resistance against taxanes partially due to alterations in tubulin genes. In this project we investigated tubulin isoforms in BC to explore any correlation between tubulin alterations and taxane resistance. Genetic alteration and expression profiling of 28 tubulin isoforms in 6714 BC tumor samples from 4205 BC cases were analyzed. Protein-protein, drug-protein and alterations neighbor genes in tubulin pathways

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Westermann, S., A. Schneider, E. K. Horn, and K. Weber. "Isolation of tubulin polyglutamylase from Crithidia; binding to microtubules and tubulin, and glutamylation of mammalian brain alpha- and beta-tubulins." Journal of Cell Science 112, no. 13 (1999): 2185–93. http://dx.doi.org/10.1242/jcs.112.13.2185.

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Trypanosomatids have a striking cage-like arrangement of submembraneous microtubules. We previously showed that alpha- and beta- tubulins of these stable microtubules are extensively modified by polyglutamylation. Cytoskeletal microtubular preparations obtained by Triton extraction of Leishmania tarentolae and Crithidia fasciculata retain an enzymatic activity that incorporates radioactive glutamic acid in a Mg2+-ATP-dependent manner into alpha- and beta-tubulins. The tubulin polyglutamylase is extracted by 0.25 M salt. The Crithidia enzyme can be purified by ATP-affinity chromatography, glyce

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Linhartová, I., P. Dráber, E. Dráberová та V. Viklický. "Immunological discrimination of β-tubulin isoforms in developing mouse brain. Post-translational modification of non-class-III β-tubulins". Biochemical Journal 288, № 3 (1992): 919–24. http://dx.doi.org/10.1042/bj2880919.

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Individual beta-tubulin isoforms in developing mouse brain were characterized using immunoblotting, after preceding high-resolution isoelectric focusing, with monoclonal antibodies against different structural regions of beta-tubulin. Some of the antibodies reacted with a limited number of tubulin isoforms in all stages of brain development and in HeLa cells. The epitope for the TU-14 antibody was located in the isotype-defining domain and was present on the beta-tubulin isotypes of classes I, II and IV, but absent on the neuron-specific class-III isotype. The data suggest that non-class-III b

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Makarova, Liubov, and Alena Korshunova. "Abstract P-36: Structural Analysis of Conformational Changes of Bacterial and Eukaryotic Tubulins." International Journal of Biomedicine 11, Suppl_1 (2021): S27—S28. http://dx.doi.org/10.21103/ijbm.11.suppl_1.p36.

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Background: Eukaryotic α- and β-tubulin proteins stand out among tubulin-like proteins by their ability to form hollow dynamically unstable microtubules (MT) with 13 protofilaments. Microtubules are part of the cell cytoskeleton and play a key role in chromosome division in mitosis. A considerable amount of anticancer drugs works on microtubules level breaking its dynamic. But the mechanism of dynamic instability and works of these drugs remains unknown. Bacteria of the genus Prostecobacter have unique bacterial tubulins (BtubA/B) capable to form hollow dynamically unstable 5 protofilament MTs

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Anders, Kirk R., та David Botstein. "Dominant-Lethal α-Tubulin Mutants Defective in Microtubule Depolymerization in Yeast". Molecular Biology of the Cell 12, № 12 (2001): 3973–86. http://dx.doi.org/10.1091/mbc.12.12.3973.

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The dynamic instability of microtubules has long been understood to depend on the hydrolysis of GTP bound to β-tubulin, an event stimulated by polymerization and necessary for depolymerization. Crystallographic studies of tubulin show that GTP is bound by β-tubulin at the longitudinal dimer-dimer interface and contacts particular α-tubulin residues in the next dimer along the protofilament. This structural arrangement suggests that these contacts could account for assembly-stimulated GTP hydrolysis. As a test of this hypothesis, we examined, in yeast cells, the effect of mutating the α-tubulin

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Morrissette, Naomi, Izra Abbaali, Chandra Ramakrishnan, and Adrian B. Hehl. "The Tubulin Superfamily in Apicomplexan Parasites." Microorganisms 11, no. 3 (2023): 706. http://dx.doi.org/10.3390/microorganisms11030706.

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Microtubules and specialized microtubule-containing structures are assembled from tubulins, an ancient superfamily of essential eukaryotic proteins. Here, we use bioinformatic approaches to analyze features of tubulins in organisms from the phylum Apicomplexa. Apicomplexans are protozoan parasites that cause a variety of human and animal infectious diseases. Individual species harbor one to four genes each for α- and β-tubulin isotypes. These may specify highly similar proteins, suggesting functional redundancy, or exhibit key differences, consistent with specialized roles. Some, but not all a

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Gudi, Radhika, Chaozhong Zou, Jun Li, and Qingshen Gao. "Centrobin–tubulin interaction is required for centriole elongation and stability." Journal of Cell Biology 193, no. 4 (2011): 711–25. http://dx.doi.org/10.1083/jcb.201006135.

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Centrobin is a daughter centriole protein that is essential for centrosome duplication. However, the molecular mechanism by which centrobin functions during centriole duplication remains undefined. In this study, we show that centrobin interacts with tubulin directly, and centrobin–tubulin interaction is pivotal for the function of centrobin during centriole duplication. We found that centrobin is recruited to the centriole biogenesis site via its interaction with tubulins during the early stage of centriole biogenesis, and its recruitment is dependent on hSAS-6 but not centrosomal P4.1–associ

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Schneider, A., T. Sherwin, R. Sasse, D. G. Russell, K. Gull, and T. Seebeck. "Subpellicular and flagellar microtubules of Trypanosoma brucei brucei contain the same alpha-tubulin isoforms." Journal of Cell Biology 104, no. 3 (1987): 431–38. http://dx.doi.org/10.1083/jcb.104.3.431.

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The cytoskeleton of the parasitic hemoflagellate Trypanosoma brucei brucei essentially consists of two microtubule-based structures: a subpellicular layer of singlet microtubules, which are in close contact with the cell membrane, and the flagellar axoneme. In addition, the cells contain a small pool of soluble tubulin. Two-dimensional gel electrophoretic analysis of the tubulins present in these subcellular compartments revealed two distinct electrophoretic isoforms of alpha-tubulin, termed alpha 1 and alpha 3. alpha 1-Tubulin most likely represents the primary translation product, while alph

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Abbaali, Izra, Danny Truong, Shania Deon Day, et al. "The tubulin database: Linking mutations, modifications, ligands and local interactions." PLOS ONE 18, no. 12 (2023): e0295279. http://dx.doi.org/10.1371/journal.pone.0295279.

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Microtubules are polymeric filaments, constructed of α-β tubulin heterodimers that underlie critical subcellular structures in eukaryotic organisms. Four homologous proteins (γ-, δ-, ε- and ζ-tubulin) additionally contribute to specialized microtubule functions. Although there is an immense volume of publicly available data pertaining to tubulins, it is difficult to assimilate all potentially relevant information across diverse organisms, isotypes, and categories of data. We previously assembled an extensive web-based catalogue of published missense mutations to tubulins with >1,500 entries

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Gaertig, J., M. A. Cruz, J. Bowen, L. Gu, D. G. Pennock, and M. A. Gorovsky. "Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila." Journal of Cell Biology 129, no. 5 (1995): 1301–10. http://dx.doi.org/10.1083/jcb.129.5.1301.

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In Tetrahymena, at least 17 distinct microtubule structures are assembled from a single primary sequence type of alpha- and beta-tubulin heterodimer, precluding distinctions among microtubular systems based on tubulin primary sequence isotypes. Tetrahymena tubulins also are modified by several types of posttranslational reactions including acetylation of alpha-tubulin at lysine 40, a modification found in most eukaryotes. In Tetrahymena, axonemal alpha-tubulin and numerous other microtubules are acetylated. We completely replaced the single type of alpha-tubulin gene in the macronucleus with a

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Fees, Colby P., та Jeffrey K. Moore. "Regulation of microtubule dynamic instability by the carboxy-terminal tail of β-tubulin". Life Science Alliance 1, № 2 (2018): e201800054. http://dx.doi.org/10.26508/lsa.201800054.

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Dynamic instability is an intrinsic property of microtubules; however, we do not understand what domains of αβ-tubulins regulate this activity or how these regulate microtubule networks in cells. Here, we define a role for the negatively charged carboxy-terminal tail (CTT) domain of β-tubulin in regulating dynamic instability. By combining in vitro studies with purified mammalian tubulin and in vivo studies with tubulin mutants in budding yeast, we demonstrate that β-tubulin CTT inhibits microtubule stability and regulates the structure and stability of microtubule plus ends. Tubulin that lack

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Li, Zhongping, Lingling Ma, Chengyong Wu, et al. "The Structure of MT189-Tubulin Complex Provides Insights into Drug Design." Letters in Drug Design & Discovery 16, no. 9 (2019): 1069–73. http://dx.doi.org/10.2174/1570180816666181122122655.

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Background: Drugs that interfere with microtubule dynamics are used widely in cancer chemotherapy. Microtubules are composed of αβ-tubulin heterodimers, and the colchicine binding site of tubulin is an important pocket for designing tubulin polymerization inhibitors. We have previously designed and synthesized a series of colchicine binding site inhibitors (CBSIs). However, these compounds showed no anticancer activity in vivo. Then, we have used a deconstruction approach to obtain a new derivative MT189, which showed in vivo anticancer activity. Methods: We crystallized a protein complex incl

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Lyons-Abbott, Sally, Dan L. Sackett, Dorota Wloga та ін. "α-Tubulin Mutations Alter Oryzalin Affinity and Microtubule Assembly Properties To Confer Dinitroaniline Resistance". Eukaryotic Cell 9, № 12 (2010): 1825–34. http://dx.doi.org/10.1128/ec.00140-10.

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ABSTRACT Plant and protozoan microtubules are selectively sensitive to dinitroanilines, which do not disrupt vertebrate or fungal microtubules. Tetrahymena thermophila is an abundant source of dinitroaniline-sensitive tubulin, and we have modified the single T. thermophila α-tubulin gene to create strains that solely express mutant α-tubulin in functional dimers. Previous research identified multiple α-tubulin mutations that confer dinitroaniline resistance in the human parasite Toxoplasma gondii, and when two of these mutations (L136F and I252L) were introduced into T. thermophila, they confe

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Zhou, Yujun, Yuanye Zhu, Yanjun Li, Yabing Duan, Rongsheng Zhang та Mingguo Zhou. "β1 Tubulin Rather Than β2 Tubulin Is the Preferred Binding Target for Carbendazim in Fusarium graminearum". Phytopathology® 106, № 9 (2016): 978–85. http://dx.doi.org/10.1094/phyto-09-15-0235-r.

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Tubulins are the proposed target of anticancer drugs, anthelminthics, and fungicides. In Fusarium graminearum, β2 tubulin has been reported to be the binding target of methyl benzimidazole carbamate (MBC) fungicides. However, the function of F. graminearum β1 tubulin, which shares 76% amino acid sequence identity with β2 tubulin, in MBC sensitivity has been unclear. In this study, MBC sensitivity relative to that of a parental strain (2021) was significantly reduced in a β1 tubulin deletion strain but increased in a β2 tubulin deletion strain, suggesting that β1 tubulin was involved in the MBC

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MacRae, Thomas H., and Carrie M. Langdon. "Tubulin synthesis, structure, and function: what are the relationships?" Biochemistry and Cell Biology 67, no. 11-12 (1989): 770–90. http://dx.doi.org/10.1139/o89-116.

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In most eukaryotes, families of tubulin genes give rise to multiple isoforms of tubulin, which may be modified post-translationally. The synthesis of isotubulins is spatially and temporally regulated, leading to the presence of different tubulins within an organism. The cellular localization of tubulin is also nonrandom with discrete isoforms residing in specific regions of some cells. Much work, dependent upon interrelated molecular and immunological technologies, has gone into determining why cells produce multiple isotubulins. One proposal would have us believe that isotubulins are function

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Garant, Katy A., та Thomas H. MacRae. "Cloning and sequencing of tubulin cDNAs from Artemia franciscana: evidence for differential expression of α- and β-tubulin genes". Biochemistry and Cell Biology 87, № 6 (2009): 989–97. http://dx.doi.org/10.1139/o09-050.

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Tubulin is a heterodimeric protein composed of α- and β-tubulin. In most organisms, they are encoded by multiple gene families whose members are subject to differential regulation. The objective of the work described herein was to better understand tubulin gene expression in the extremophile Artemia franciscana To this end tubulin cDNAs were cloned and sequenced. αAT2, an α-tubulin cDNA, differed by one nucleotide from αAT1, a previously cloned Artemia cDNA. This change, possibly generated by allelic variation, caused an M313V substitution in α-tubulin. The amino acid sequence of β-tubulin enc

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