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Artículos de revistas sobre el tema "Tubulins"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 29 de julio de 2024

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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 (September 1, 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

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 (March 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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3

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 (March 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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4

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 (January 6, 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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5

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 (August 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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6

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 (June 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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7

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 (June 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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8

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 (February 12, 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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9

Lajoie-Mazenc, I., C. Detraves, V. Rotaru, M. Gares, Y. Tollon, C. Jean, M. Julian, M. Wright, and B. Raynaud-Messina. "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 (October 1, 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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10

Chumová, Jana, Hana Kourová, Lucie Trögelová, Petr Halada та Pavla Binarová. "Microtubular and Nuclear Functions of γ-Tubulin: Are They LINCed?" Cells 8, № 3 (19 березня 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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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 (February 15, 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

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 (August 1, 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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13

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 (June 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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14

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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15

Chu, Chih-Wen, Fajian Hou, Junmei Zhang, Lilian Phu, Alex V. Loktev, Donald S. Kirkpatrick, Peter K. Jackson, Yingming Zhao та Hui Zou. "A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation". Molecular Biology of the Cell 22, № 4 (15 лютого 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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16

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 (July 1, 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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17

Burke, D., P. Gasdaska, and L. Hartwell. "Dominant effects of tubulin overexpression in Saccharomyces cerevisiae." Molecular and Cellular Biology 9, no. 3 (March 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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18

Burke, D., P. Gasdaska, and L. Hartwell. "Dominant effects of tubulin overexpression in Saccharomyces cerevisiae." Molecular and Cellular Biology 9, no. 3 (March 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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19

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 (January 15, 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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20

Yu, Nuo, and Niels Galjart. "TAPping into the treasures of tubulin using novel protein production methods." Essays in Biochemistry 62, no. 6 (November 14, 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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21

Kristensson, Maria Alvarado. "The Game of Tubulins." Cells 10, no. 4 (March 28, 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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22

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 (лютий 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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23

Hecht, N. B., R. J. Distel, P. C. Yelick, S. M. Tanhauser, C. E. Driscoll, E. Goldberg, and K. S. Tung. "Localization of a highly divergent mammalian testicular alpha tubulin that is not detectable in brain." Molecular and Cellular Biology 8, no. 2 (February 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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24

Hecht, N. B., R. J. Distel, P. C. Yelick, S. M. Tanhauser, C. E. Driscoll, E. Goldberg, and K. S. Tung. "Localization of a highly divergent mammalian testicular alpha tubulin that is not detectable in brain." Molecular and Cellular Biology 8, no. 2 (February 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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25

Lin, Zhewang, Ivana Gasic, Viswanathan Chandrasekaran, Niklas Peters, Sichen Shao, Timothy J. Mitchison, and Ramanujan S. Hegde. "TTC5 mediates autoregulation of tubulin via mRNA degradation." Science 367, no. 6473 (November 14, 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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26

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 (January 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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27

Ragusa, Maria Antonietta, Aldo Nicosia, Salvatore Costa, Caterina Casano, and Fabrizio Gianguzza. "A Survey on Tubulin and Arginine Methyltransferase Families Sheds Light on P. lividus Embryo as Model System for Antiproliferative Drug Development." International Journal of Molecular Sciences 20, no. 9 (April 30, 2019): 2136. http://dx.doi.org/10.3390/ijms20092136.

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Tubulins and microtubules (MTs) represent targets for taxane-based chemotherapy. To date, several lines of evidence suggest that effectiveness of compounds binding tubulin often relies on different post-translational modifications on tubulins. Among them, methylation was recently associated to drug resistance mechanisms impairing taxanes binding. The sea urchin is recognized as a research model in several fields including fertilization, embryo development and toxicology. To date, some α- and β-tubulin genes have been identified in P. lividus, while no data are available in echinoderms for argi

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28

Morrissette, Naomi, Izra Abbaali, Chandra Ramakrishnan, and Adrian B. Hehl. "The Tubulin Superfamily in Apicomplexan Parasites." Microorganisms 11, no. 3 (March 9, 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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29

Wick, S. "Maize beta tubulin genes and beta tubulins." Cell Biology International 27, no. 3 (2003): 301. http://dx.doi.org/10.1016/s1065-6995(02)00332-3.

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30

Kubo, Tomohiro, and Toshiyuki Oda. "Electrostatic interaction between polyglutamylated tubulin and the nexin–dynein regulatory complex regulates flagellar motility." Molecular Biology of the Cell 28, no. 17 (August 15, 2017): 2260–66. http://dx.doi.org/10.1091/mbc.e17-05-0285.

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Tubulins undergo various posttranslational modifications. Among them, polyglutamylation is involved in the motility of eukaryotic flagella and the stability of the axonemal microtubules. However, it remains unclear where polyglutamylated tubulin localizes precisely within the axoneme and how tubulin polyglutamylation affects flagellar motility. In this study, we identified the three-dimensional localization of the polyglutamylated tubulin in Chlamydomonas flagella using antibody labeling and cryo–electron tomography. Polyglutamylated tubulins specifically located in close proximity to a microt

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31

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 (January 5, 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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32

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 (15 грудня 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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33

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 (September 1, 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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34

SULIMENKO, Vadym, Tetyana SULIMENKO, Slobodan POZNANOVIC, Volodymyr NECHIPORUK-ZLOY, Konrad J. BÖHM, Libor MACUREK, Eberhard UNGER та Pavel DRÁBER. "Association of brain γ-tubulins with αβ-tubulin dimers". Biochemical Journal 365, № 3 (1 серпня 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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35

Vaughan, Susan, Terri Attwood, Miguel Navarro, Valerie Scott, Paul McKean, Andrea Baines, and Keith Gull. "Tubulins in Parasite Protozoa: Epsilon and Zeta Tubulin." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A218. http://dx.doi.org/10.1042/bst028a218a.

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36

Chin, Hang Gyeong, Pierre-Olivier Esteve, Cristian Ruse, Jiyoung Lee, Scott E. Schaus, Sriharsa Pradhan та Ulla Hansen. "The microtubule-associated histone methyltransferase SET8, facilitated by transcription factor LSF, methylates α-tubulin". Journal of Biological Chemistry 295, № 14 (28 лютого 2020): 4748–59. http://dx.doi.org/10.1074/jbc.ra119.010951.

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Microtubules are cytoskeletal structures critical for mitosis, cell motility, and protein and organelle transport and are a validated target for anticancer drugs. However, how tubulins are regulated and recruited to support these distinct cellular processes is incompletely understood. Posttranslational modifications of tubulins are proposed to regulate microtubule function and dynamics. Although many of these modifications have been investigated, only one prior study reports tubulin methylation and an enzyme responsible for this methylation. Here we used in vitro radiolabeling, MS, and immunob

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37

Kollman, Justin M., Alex Zelter, Eric G. D. Muller, Bethany Fox, Luke M. Rice, Trisha N. Davis та David A. Agard. "The Structure of the γ-Tubulin Small Complex: Implications of Its Architecture and Flexibility for Microtubule Nucleation". Molecular Biology of the Cell 19, № 1 (січень 2008): 207–15. http://dx.doi.org/10.1091/mbc.e07-09-0879.

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The γ-tubulin small complex (γ-TuSC) is an evolutionarily conserved heterotetramer essential for microtubule nucleation. We have determined the structure of the Saccharomyces cerevisiae γ-TuSC at 25-Å resolution by electron microscopy. γ-TuSC is Y-shaped, with an elongated body connected to two arms. Gold labeling showed that the two γ-tubulins are located in lobes at the ends of the arms, and the relative orientations of the other γ-TuSC components were determined by in vivo FRET. The structures of different subpopulations of γ-TuSC indicate flexibility in the connection between a mobile arm

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38

Million, K., J. Larcher, J. Laoukili, D. Bourguignon, F. Marano, and F. Tournier. "Polyglutamylation and polyglycylation of alpha- and beta-tubulins during in vitro ciliated cell differentiation of human respiratory epithelial cells." Journal of Cell Science 112, no. 23 (December 1, 1999): 4357–66. http://dx.doi.org/10.1242/jcs.112.23.4357.

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Tubulins are the major proteins within centriolar and axonemal structures. In all cell types studied so far, numerous alpha- and beta-tubulin isoforms are generated both by expression of a multigenic family and various post-translational modifications. We have developed a primary culture of human nasal epithelial cells where the ciliated cell differentiation process has been observed and quantified. We have used this system to study several properties concerning polyglutamylation and polyglycylation of tubulin. GT335, a monoclonal antibody directed against glutamylated tubulins, stained the ce

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39

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 (December 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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40

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 (December 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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41

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 (May 16, 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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42

Pratt, L. F., S. Okamura, and D. W. Cleveland. "A divergent testis-specific alpha-tubulin isotype that does not contain a coded C-terminal tyrosine." Molecular and Cellular Biology 7, no. 1 (January 1987): 552–55. http://dx.doi.org/10.1128/mcb.7.1.552-555.1987.

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On the basis of analysis of cDNA clones of alpha-tubulin RNAs expressed during spermiogenesis in chickens, we report the identification of a novel alpha-tubulin which is expressed exclusively in chicken testes. Comparison of its sequence with those previously determined not only demonstrates that the encoded polypeptide is significantly divergent from other alpha-tubulins but also supports the hypothesis that alpha-tubulin isotypes are distinguished by a carboxy-terminal variable region sequence and, to a lesser extent, by a domain near the amino terminus. Since essentially all previously know

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43

Pratt, L. F., S. Okamura, and D. W. Cleveland. "A divergent testis-specific alpha-tubulin isotype that does not contain a coded C-terminal tyrosine." Molecular and Cellular Biology 7, no. 1 (January 1987): 552–55. http://dx.doi.org/10.1128/mcb.7.1.552.

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On the basis of analysis of cDNA clones of alpha-tubulin RNAs expressed during spermiogenesis in chickens, we report the identification of a novel alpha-tubulin which is expressed exclusively in chicken testes. Comparison of its sequence with those previously determined not only demonstrates that the encoded polypeptide is significantly divergent from other alpha-tubulins but also supports the hypothesis that alpha-tubulin isotypes are distinguished by a carboxy-terminal variable region sequence and, to a lesser extent, by a domain near the amino terminus. Since essentially all previously know

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44

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 (16 травня 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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45

Ruiz, F., P. Dupuis-Williams, C. Klotz, F. Forquignon, M. Bergdoll, J. Beisson та F. Koll. "Genetic Evidence for Interaction between η- and β-Tubulins". Eukaryotic Cell 3, № 1 (лютий 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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46

Fackenthal, J. D., J. A. Hutchens, F. R. Turner, and E. C. Raff. "Structural analysis of mutations in the Drosophila beta 2-tubulin isoform reveals regions in the beta-tubulin molecular required for general and for tissue-specific microtubule functions." Genetics 139, no. 1 (January 1, 1995): 267–86. http://dx.doi.org/10.1093/genetics/139.1.267.

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Abstract We have determined the lesions in a number of mutant alleles of beta Tub85D, the gene that encodes the testis-specific beta 2-tubulin isoform in Drosophila melanogaster. Mutations responsible for different classes of functional phenotypes are distributed throughout the beta 2-tubulin molecule. There is a telling correlation between the degree of phylogenetic conservation of the altered residues and the number of different microtubule categories disrupted by the lesions. The majority of lesions occur at positions that are evolutionarily highly conserved in all beta-tubulins; these lesi

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47

Gu, Ying, Zhiping Deng, Alexander R. Paredez, Seth DeBolt, Zhi-Yong Wang, and Chris Somerville. "Prefoldin 6 is required for normal microtubule dynamics and organization in Arabidopsis." Proceedings of the National Academy of Sciences 105, no. 46 (November 11, 2008): 18064–69. http://dx.doi.org/10.1073/pnas.0808652105.

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Newly translated tubulin molecules undergo a series of complex interactions with nascent chain-binding chaperones, including prefoldin (PFD) and chaperonin-containing TCP-1 (CCT). By screening for oryzalin hypersensitivity, we identified several mutants of Arabidopsis that have lesions in PFD subunits. The pfd6–1 mutant exhibits a range of microtubule defects, including hypersensitivity to oryzalin, defects in cell division, cortical array organization, and microtubule dynamicity. Consistent with phenotypic analysis, proteomic analysis indicates several isoforms of tubulins were reduced in pfd

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48

Katz, W. S., and F. Solomon. "Diversity among beta-tubulins: a carboxy-terminal domain of yeast beta-tubulin is not essential in vivo." Molecular and Cellular Biology 8, no. 7 (July 1988): 2730–36. http://dx.doi.org/10.1128/mcb.8.7.2730-2736.1988.

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Sequences of genes for beta-tubulins from many different organisms demonstrate that they encode highly conserved proteins but that these proteins diverge considerably at their carboxyl termini. The patterns of interspecies conservation of this diversity suggest that it may have functional significance. We have taken advantage of the properties of Saccharomyces cerevisiae to test this hypothesis in vivo. The sole beta-tubulin gene of this species is one of the most divergent of all beta-tubulins and encodes 12 amino acids which extend past the end of most other beta-tubulin molecules. We have c

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49

Katz, W. S., and F. Solomon. "Diversity among beta-tubulins: a carboxy-terminal domain of yeast beta-tubulin is not essential in vivo." Molecular and Cellular Biology 8, no. 7 (July 1988): 2730–36. http://dx.doi.org/10.1128/mcb.8.7.2730.

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Sequences of genes for beta-tubulins from many different organisms demonstrate that they encode highly conserved proteins but that these proteins diverge considerably at their carboxyl termini. The patterns of interspecies conservation of this diversity suggest that it may have functional significance. We have taken advantage of the properties of Saccharomyces cerevisiae to test this hypothesis in vivo. The sole beta-tubulin gene of this species is one of the most divergent of all beta-tubulins and encodes 12 amino acids which extend past the end of most other beta-tubulin molecules. We have c

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50

Abbaali, Izra, Danny Truong, Shania Deon Day, Faliha Mushayeed, Bhargavi Ganesh, Nancy Haro-Ramirez, Juliet Isles, et al. "The tubulin database: Linking mutations, modifications, ligands and local interactions." PLOS ONE 18, no. 12 (December 8, 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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