메뉴 건너뛰기




Volumn 73, Issue 4, 1997, Pages 306-315

Ortho-vanadate affects both the tyrosination/detyrosination state of spindle microtubules and the organization of XTH-2 spindles

Author keywords

Amphibian cell line; monoclonal antibodies; o vanadate; Posttranslationally modified tubulin; Spindle organization

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE; ORTHOVANADIC ACID; TUBULIN;

EID: 0030768604     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (14)

References (49)
  • 1
    • 0027230133 scopus 로고
    • Astral and spindle forces in PtK2 cells during anaphase B: A laser microbeam study
    • Aist, J., H. Liang, M. W. Berns: Astral and spindle forces in PtK2 cells during anaphase B: a laser microbeam study. J. Cell Sci. 104, 1207-1216 (1993).
    • (1993) J. Cell Sci. , vol.104 , pp. 1207-1216
    • Aist, J.1    Liang, H.2    Berns, M.W.3
  • 2
    • 0026047352 scopus 로고
    • Direct experimental evidence for the existence, structural basis and function of astral forces during anaphase B in vivo
    • Aist, J. R., C. J. Bayles, W. Tao, M. W. Berns: Direct experimental evidence for the existence, structural basis and function of astral forces during anaphase B in vivo. J. Cell Sci. 100, 279-288 (1991).
    • (1991) J. Cell Sci. , vol.100 , pp. 279-288
    • Aist, J.R.1    Bayles, C.J.2    Tao, W.3    Berns, M.W.4
  • 3
    • 0024020919 scopus 로고
    • Posttranslational tyrosination/detyrosination of tubulin
    • Barra, H. S., C. A. Arce, C. E. Argarana: Posttranslational tyrosination/detyrosination of tubulin. Mol. Neurobiol 2, 133-153 (1988).
    • (1988) Mol. Neurobiol , vol.2 , pp. 133-153
    • Barra, H.S.1    Arce, C.A.2    Argarana, C.E.3
  • 4
    • 0026181461 scopus 로고
    • Stabilization and posttranslational modification of microtubules during cellular morphogenesis
    • Bulinski, J. C., G. G. Gundersen: Stabilization and posttranslational modification of microtubules during cellular morphogenesis. BioEssays 13, 285-293 (1991).
    • (1991) BioEssays , vol.13 , pp. 285-293
    • Bulinski, J.C.1    Gundersen, G.G.2
  • 5
    • 0023947838 scopus 로고
    • Post-translational modifications of α-tubulin: Detyrosylation and acetylation differentiate populations of interphase microtubules in cultured cells
    • Bulinski, J. C., J. E. Richards, G. Piperno: Post-translational modifications of α-tubulin: Detyrosylation and acetylation differentiate populations of interphase microtubules in cultured cells. J. Cell Biol. 106, 1213-1220 (1988).
    • (1988) J. Cell Biol. , vol.106 , pp. 1213-1220
    • Bulinski, J.C.1    Richards, J.E.2    Piperno, G.3
  • 6
    • 0020066965 scopus 로고
    • Nucleotide requirements for anaphase chromosome movements in permeabilized mitotic cells: Anaphase B but not anaphase a requires ATP
    • Cande, W. Z.: Nucleotide requirements for anaphase chromosome movements in permeabilized mitotic cells: Anaphase B but not anaphase A requires ATP. Cell 28, 15-22 (1982).
    • (1982) Cell , vol.28 , pp. 15-22
    • Cande, W.Z.1
  • 7
    • 0018136985 scopus 로고
    • Chromosome movement in lysed mitotic cells is inhibited by vanadate
    • Cande, W. Z., S. M. Wolniak: Chromosome movement in lysed mitotic cells is inhibited by vanadate. J. Cell Biol. 79, 573-580 (1978).
    • (1978) J. Cell Biol. , vol.79 , pp. 573-580
    • Cande, W.Z.1    Wolniak, S.M.2
  • 8
    • 0028557424 scopus 로고
    • Tyrosine phosphorylation is involved in reorganization of the actin cytoskeleton in response to serum or LPA stimulation
    • Chrzanowska-Wodnicka, M., K. Burridge: Tyrosine phosphorylation is involved in reorganization of the actin cytoskeleton in response to serum or LPA stimulation. J. Cell Sci. 107, 3643-3654 (1994).
    • (1994) J. Cell Sci. , vol.107 , pp. 3643-3654
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 9
    • 0021891876 scopus 로고
    • Molecular biology and genetics of tubulin
    • Cleveland, D. W., K. F. Sullivan: Molecular biology and genetics of tubulin. Annu. Rev. Biochem. 54, 331-365 (1985).
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 331-365
    • Cleveland, D.W.1    Sullivan, K.F.2
  • 10
    • 0001165632 scopus 로고
    • In vivo effects of ortho-vanadate on spindle structure and dynamics of locust spermatocytes I
    • Daub, A., M. Hauser: In vivo effects of ortho-vanadate on spindle structure and dynamics of locust spermatocytes I. Chromosoma 93, 271-280 (1986).
    • (1986) Chromosoma , vol.93 , pp. 271-280
    • Daub, A.1    Hauser, M.2
  • 11
    • 0027210758 scopus 로고
    • Okadaic acid induces spindle lengthening and disrupts the interaction of microtubules with the kinetochores in metapase II-arrested mouse oocytes
    • De Pennart, H., M. H. Verlhac, C. Cibert, A. Santa Maria, B. Maro: Okadaic acid induces spindle lengthening and disrupts the interaction of microtubules with the kinetochores in metapase II-arrested mouse oocytes. Dev. Biol. 157, 170-181 (1993).
    • (1993) Dev. Biol. , vol.157 , pp. 170-181
    • De Pennart, H.1    Verlhac, M.H.2    Cibert, C.3    Santa Maria, A.4    Maro, B.5
  • 12
    • 0026556757 scopus 로고
    • Cdc2 kinase-induced destabilization of MAP2-coated microtubules
    • Faruki, S., M. Doree, E. Karsenti: Cdc2 kinase-induced destabilization of MAP2-coated microtubules. J. Cell Sci. 101, 69-78 (1992).
    • (1992) J. Cell Sci. , vol.101 , pp. 69-78
    • Faruki, S.1    Doree, M.2    Karsenti, E.3
  • 13
    • 0021990889 scopus 로고
    • A polymer-dependent increase in phosphorylation of β-tubulin accompanies differentiations of a mouse neuroblastoma cell line
    • Gard D. L., M. W. Kirschner: A polymer-dependent increase in phosphorylation of β-tubulin accompanies differentiations of a mouse neuroblastoma cell line. J. Cell Biol. 100, 764-774 (1985).
    • (1985) J. Cell Biol. , vol.100 , pp. 764-774
    • Gard, D.L.1    Kirschner, M.W.2
  • 14
    • 0022976646 scopus 로고
    • Ultrastructural Colocalization of Tyrosinated and Detyrosinated α-tubulin in interphase and mitotic cells
    • Geuens, G., G. G. Gundersen, R. Nuydens, F. Cornelissen, J. C. Bulinski, M. De Brabander: Ultrastructural Colocalization of Tyrosinated and Detyrosinated α-tubulin in interphase and mitotic cells. J. Cell Biol. 103, 1883-1893 (1986).
    • (1986) J. Cell Biol. , vol.103 , pp. 1883-1893
    • Geuens, G.1    Gundersen, G.G.2    Nuydens, R.3    Cornelissen, F.4    Bulinski, J.C.5    De Brabander, M.6
  • 16
    • 0001064670 scopus 로고
    • Inhibition of myosin ATPase by vanadate ion
    • Goodno, C. C., Inhibition of myosin ATPase by vanadate ion. Proc. Natl. Acad. Sci. USA 76, 2620-2624 (1979).
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2620-2624
    • Goodno, C.C.1
  • 17
    • 0025953405 scopus 로고
    • Use of vanadate as protein-phosphotyrosine phosphatase inhibitor
    • Gordon, J. A., Use of vanadate as protein-phosphotyrosine phosphatase inhibitor. Methods Enzymol. 201, 477-482 (1991).
    • (1991) Methods Enzymol. , vol.201 , pp. 477-482
    • Gordon, J.A.1
  • 19
    • 0011317720 scopus 로고
    • The interaction of vanadate with tyrosine kinases and phosphatases
    • Gresser, M. J., A. A. Tracey, P. J. Stankiewicz: The interaction of vanadate with tyrosine kinases and phosphatases. Adv. Prot. Phosphatases 4, 35-57 (1987).
    • (1987) Adv. Prot. Phosphatases , vol.4 , pp. 35-57
    • Gresser, M.J.1    Tracey, A.A.2    Stankiewicz, P.J.3
  • 20
    • 0022501223 scopus 로고
    • Distribution of tyrosinated and nontyrosinated α-tubulin during mitosis
    • Gundersen, G. G., J. C. Bulinski: Distribution of tyrosinated and nontyrosinated α-tubulin during mitosis. J. Cell Biol. 102, 1118-1126 (1986).
    • (1986) J. Cell Biol. , vol.102 , pp. 1118-1126
    • Gundersen, G.G.1    Bulinski, J.C.2
  • 21
    • 0005940728 scopus 로고
    • Microtubules enriched in detyrosinated tubulin in vivo are less dynamic than those enriched in tyrosinated tubulin
    • J. Arechaga, R. Maccioni (eds.). ICSU Press. Miami
    • Gundersen, G. G., S. Khawaja, J. C. Bulinski: Microtubules enriched in detyrosinated tubulin in vivo are less dynamic than those enriched in tyrosinated tubulin. In: J. Arechaga, R. Maccioni (eds.): The Cytoskeleton and Cell Differentiation and Development, pp. 75-81. ICSU Press. Miami 1987.
    • (1987) The Cytoskeleton and Cell Differentiation and Development , pp. 75-81
    • Gundersen, G.G.1    Khawaja, S.2    Bulinski, J.C.3
  • 22
    • 84939272462 scopus 로고
    • Vanadate inhibits anaphase a as well as anaphase B
    • Hanke-Bücker, G., M. Hauser: Vanadate inhibits anaphase A as well as anaphase B. Eur. J. Cell Biol. 60 (Suppl. 37), 440 (1993).
    • (1993) Eur. J. Cell Biol. , vol.60 , Issue.37 SUPPL. , pp. 440
    • Hanke-Bücker, G.1    Hauser, M.2
  • 23
    • 0021680449 scopus 로고
    • Cytoplasmic dynein-like ATPase crosslinks microtubules in an ATP-sensitive manner
    • Hollenbek, P. J., F. Suprynowicz, W. Z. Cande: Cytoplasmic dynein-like ATPase crosslinks microtubules in an ATP-sensitive manner. J. Cell Biol. 99, 1251-1258 (1984).
    • (1984) J. Cell Biol. , vol.99 , pp. 1251-1258
    • Hollenbek, P.J.1    Suprynowicz, F.2    Cande, W.Z.3
  • 24
    • 0023877365 scopus 로고
    • Enhanced stability of microtubules enriched in detyrosinated tubulin is not a direct function of detyrosination level
    • Khawaja, S., G. G. Gundersen, J. C. Bulinski: Enhanced stability of microtubules enriched in detyrosinated tubulin is not a direct function of detyrosination level. J. Cell Biol. 106, 141-149 (1988).
    • (1988) J. Cell Biol. , vol.106 , pp. 141-149
    • Khawaja, S.1    Gundersen, G.G.2    Bulinski, J.C.3
  • 25
    • 0020265993 scopus 로고
    • Rat monoclonal antitubulin antibodies derived by using a nonsecreting rat cell line
    • Kilmartin, J. V., B. Wright, C. Milstein: Rat monoclonal antitubulin antibodies derived by using a nonsecreting rat cell line. J. Cell Biol. 93, 576-582 (1982).
    • (1982) J. Cell Biol. , vol.93 , pp. 576-582
    • Kilmartin, J.V.1    Wright, B.2    Milstein, C.3
  • 26
    • 0022760661 scopus 로고
    • Reactivation of organelle movements along the cytoskeletal framework of a giant freshwater ameba
    • Koonce, M. P., M. Schliwa: Reactivation of organelle movements along the cytoskeletal framework of a giant freshwater ameba. J. Cell Biol. 103, 605-612 (1986).
    • (1986) J. Cell Biol. , vol.103 , pp. 605-612
    • Koonce, M.P.1    Schliwa, M.2
  • 27
    • 0023403268 scopus 로고
    • Microtubules containing detyrosinated tubulin are less dynamic
    • Kreis, T. E.: Microtubules containing detyrosinated tubulin are less dynamic. EMBO J. 6, 2597-2606 (1987).
    • (1987) EMBO J. , vol.6 , pp. 2597-2606
    • Kreis, T.E.1
  • 29
  • 30
    • 0012609671 scopus 로고
    • The cytoskeleton of Reticulomyxa filosa reticulopodia contains Glu-tubulin as a main component
    • Lindenblatt, J., N. Hülsmann, M. Hauser: The cytoskeleton of Reticulomyxa filosa reticulopodia contains Glu-tubulin as a main component. Eur. J. Protistol. 25, 145-157 (1989).
    • (1989) Eur. J. Protistol. , vol.25 , pp. 145-157
    • Lindenblatt, J.1    Hülsmann, N.2    Hauser, M.3
  • 31
    • 0024369644 scopus 로고
    • Polewards microtubule flux in the mitotic spindle: Evidence from photoactivation of fluorescence
    • Mitchison, T. J.: Polewards microtubule flux in the mitotic spindle: Evidence from photoactivation of fluorescence. J. Cell Biol. 109, 637-652 (1989).
    • (1989) J. Cell Biol. , vol.109 , pp. 637-652
    • Mitchison, T.J.1
  • 32
    • 0021287515 scopus 로고
    • Mechanisms of action of vanadium
    • Nechay, B. R.: Mechanisms of action of vanadium. Pharmacol. Toxicol. 24, 501-514 (1984).
    • (1984) Pharmacol. Toxicol. , vol.24 , pp. 501-514
    • Nechay, B.R.1
  • 33
    • 0023608935 scopus 로고
    • MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
    • Paschal, B. M., H. S. Shpetner, R. B. Vallee: MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. J. Cell Biol. 105, 1273-1282 (1987).
    • (1987) J. Cell Biol. , vol.105 , pp. 1273-1282
    • Paschal, B.M.1    Shpetner, H.S.2    Vallee, R.B.3
  • 35
    • 0026766356 scopus 로고
    • A thousand and two protein tyrosine phosphatases
    • Pot, D. A., J. E. Dixon: A thousand and two protein tyrosine phosphatases. Biochim. Biophys. Acta 1136, 35-43 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1136 , pp. 35-43
    • Pot, D.A.1    Dixon, J.E.2
  • 37
    • 2042497577 scopus 로고
    • Established Xenopus tadpole heart endothelium (XTH) cells exhibiting selected properties of primary cells
    • Abstract
    • Schlage, W. K., J. Bereiter-Hahn, C. Kuhn: Established Xenopus tadpole heart endothelium (XTH) cells exhibiting selected properties of primary cells. Eur. J. Cell Biol. 24, No. 2, Abstract p. 21 (1981).
    • (1981) Eur. J. Cell Biol. , vol.24 , Issue.2 , pp. 21
    • Schlage, W.K.1    Bereiter-Hahn, J.2    Kuhn, C.3
  • 38
    • 0022371050 scopus 로고
    • Identification of kinesin in sea urchin eggs, and evidence for its localization in the mitotic spindle
    • Scholey, J. M., M. E. Porter, P. M. Grissom, J. R. McIntosh: Identification of kinesin in sea urchin eggs, and evidence for its localization in the mitotic spindle. Nature 318, 483-486 (1985).
    • (1985) Nature , vol.318 , pp. 483-486
    • Scholey, J.M.1    Porter, M.E.2    Grissom, P.M.3    McIntosh, J.R.4
  • 39
    • 0021999029 scopus 로고
    • Polymerization of tubulin in vivo: Direct evidence for assembly onto microtubule ends and from centrosomes
    • Soltys, B. J., G. G. Borisy: Polymerization of tubulin in vivo: direct evidence for assembly onto microtubule ends and from centrosomes. J. Cell Biol. 100, 1682-1689 (1985).
    • (1985) J. Cell Biol. , vol.100 , pp. 1682-1689
    • Soltys, B.J.1    Borisy, G.G.2
  • 40
    • 0024284753 scopus 로고
    • Inhibition of phosphatase and sulfatase by transition-state analogues
    • Stankiewicz, P. J., M. Gresser: Inhibition of phosphatase and sulfatase by transition-state analogues. Biochemistry 27, 206-212 (1988).
    • (1988) Biochemistry , vol.27 , pp. 206-212
    • Stankiewicz, P.J.1    Gresser, M.2
  • 41
    • 0025320820 scopus 로고
    • Localization of cytoplasmic dynein to mitotic spindles and kinetochores
    • Steuer, E. R., L. Wordeman, T. A. Schroer, M. P. Sheetz: Localization of cytoplasmic dynein to mitotic spindles and kinetochores. Nature 345, 266-268 (1990).
    • (1990) Nature , vol.345 , pp. 266-268
    • Steuer, E.R.1    Wordeman, L.2    Schroer, T.A.3    Sheetz, M.P.4
  • 42
    • 0024430932 scopus 로고
    • Anaphase onset and dephosphorylation of mitotic phosphoproteins occur concomitantly
    • Vandre, D. D., G. G. Borisy: Anaphase onset and dephosphorylation of mitotic phosphoproteins occur concomitantly. J. Cell Sci. 94, 245-258 (1989).
    • (1989) J. Cell Sci. , vol.94 , pp. 245-258
    • Vandre, D.D.1    Borisy, G.G.2
  • 43
    • 0026542842 scopus 로고
    • Inhibition of mitosis by okadaic acid: Possible involvement of a protein phosphatase 2a in the transition from metaphase to anaphase
    • Vandre, D. D., V. L. Wills: Inhibition of mitosis by okadaic acid: possible involvement of a protein phosphatase 2A in the transition from metaphase to anaphase. J. Cell Sci. 101, 79-91 (1992).
    • (1992) J. Cell Sci. , vol.101 , pp. 79-91
    • Vandre, D.D.1    Wills, V.L.2
  • 44
    • 0022460613 scopus 로고
    • Analysis of the treadmilling model during metaphase of mitosis using fluorescence distribution after photobleaching
    • Wadsworth, P., E. D. Salmon: Analysis of the treadmilling model during metaphase of mitosis using fluorescence distribution after photobleaching. J. Cell Biol. 102, 1032-1038 (1986).
    • (1986) J. Cell Biol. , vol.102 , pp. 1032-1038
    • Wadsworth, P.1    Salmon, E.D.2
  • 45
    • 0025006680 scopus 로고
    • Distribution of microtubules containing post-translationally modified α-tubulin during Drosophila embryogenesis
    • Warn, R. M., A. Harrison, V. Planques, N. Robert-Nicoud, J. Wehland: Distribution of microtubules containing post-translationally modified α-tubulin during Drosophila embryogenesis. Cell Motil. Cytoskeleton 17, 34-45 (1990).
    • (1990) Cell Motil. Cytoskeleton , vol.17 , pp. 34-45
    • Warn, R.M.1    Harrison, A.2    Planques, V.3    Robert-Nicoud, N.4    Wehland, J.5
  • 46
    • 18844475127 scopus 로고
    • Microtubules are acetylated in domains that turn over slowly
    • Webster, D. R., G. G. Borisy: Microtubules are acetylated in domains that turn over slowly. J. Cell Sci. 92, 57-62 (1989).
    • (1989) J. Cell Sci. , vol.92 , pp. 57-62
    • Webster, D.R.1    Borisy, G.G.2
  • 48
    • 0023406178 scopus 로고
    • Turnover of the carboxy-terminal tyrosine of α-tubulin and means of reaching elevated levels of detyrosination in living cells
    • Wehland, J., K. Weber: Turnover of the carboxy-terminal tyrosine of α-tubulin and means of reaching elevated levels of detyrosination in living cells. J. Cell Sci. 88, 185-203 (1987).
    • (1987) J. Cell Sci. , vol.88 , pp. 185-203
    • Wehland, J.1    Weber, K.2
  • 49
    • 0021074286 scopus 로고
    • A rat monoclonal antibody reacting specifically with the tyrosylated form of α-tubulin. I. Biochemical characterization, effects on microtubule polymerization in vitro, and microtubule polymerization and organization in vivo
    • Wehland, J., M. C. Willingham, I. V. Sandoval: A rat monoclonal antibody reacting specifically with the tyrosylated form of α-tubulin. I. Biochemical characterization, effects on microtubule polymerization in vitro, and microtubule polymerization and organization in vivo. J. Cell Biol. 97, 1467-1475 (1983).
    • (1983) J. Cell Biol. , vol.97 , pp. 1467-1475
    • Wehland, J.1    Willingham, M.C.2    Sandoval, I.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.