메뉴 건너뛰기




Volumn 70, Issue 12, 2013, Pages 849-862

Paclitaxel resistance by random mutagenesis of α-tubulin

Author keywords

Cancer; Drug resistance; Microtubules; Mitosis; Multinucleation; Neurological defects; Taxanes; Vinblastine

Indexed keywords

ALPHA TUBULIN; COMPLEMENTARY DNA; GENOMIC DNA; PACLITAXEL;

EID: 84890180718     PISSN: 19493584     EISSN: 19493592     Source Type: Journal    
DOI: 10.1002/cm.21154     Document Type: Article
Times cited : (18)

References (57)
  • 1
    • 0020601397 scopus 로고
    • Mutations in α- and β-tubulin affect spindle formation in Chinese hamster ovary cells
    • Abraham I, Marcus M, Cabral F, Gottesman MM. 1983. Mutations in α- and β-tubulin affect spindle formation in Chinese hamster ovary cells. J Cell Biol 97:1055-1061.
    • (1983) J Cell Biol , vol.97 , pp. 1055-1061
    • Abraham, I.1    Marcus, M.2    Cabral, F.3    Gottesman, M.M.4
  • 3
    • 80053457091 scopus 로고    scopus 로고
    • Mutations in the beta-tubulin binding site for peloruside A confer resistance by targeting a cleft significant in side chain binding
    • Begaye A, Trostel S, Zhao Z, Taylor RE, Schriemer DC, Sackett DL. 2011. Mutations in the beta-tubulin binding site for peloruside A confer resistance by targeting a cleft significant in side chain binding. Cell Cycle 10:3387-3396.
    • (2011) Cell Cycle , vol.10 , pp. 3387-3396
    • Begaye, A.1    Trostel, S.2    Zhao, Z.3    Taylor, R.E.4    Schriemer, D.C.5    Sackett, D.L.6
  • 4
    • 3042803372 scopus 로고    scopus 로고
    • A ubiquitous β-tubulin disrupts microtubule assembly and inhibits cell proliferation
    • Bhattacharya R, Cabral F. 2004. A ubiquitous β-tubulin disrupts microtubule assembly and inhibits cell proliferation. Mol Biol Cell 15:3123-3131.
    • (2004) Mol Biol Cell , vol.15 , pp. 3123-3131
    • Bhattacharya, R.1    Cabral, F.2
  • 5
    • 0023391463 scopus 로고
    • Mutations affecting assembly and stability of tubulin: Evidence for a non-essential β-tubulin in CHO cells
    • Boggs B, Cabral F. 1987. Mutations affecting assembly and stability of tubulin: Evidence for a non-essential β-tubulin in CHO cells. Mol Cell Biol 7:2700-2707.
    • (1987) Mol Cell Biol , vol.7 , pp. 2700-2707
    • Boggs, B.1    Cabral, F.2
  • 6
    • 0020583997 scopus 로고
    • Isolation of Chinese hamster ovary cell mutants requiring the continuous presence of taxol for cell division
    • Cabral F. 1983. Isolation of Chinese hamster ovary cell mutants requiring the continuous presence of taxol for cell division. J Cell Biol 97:22-29.
    • (1983) J Cell Biol , vol.97 , pp. 22-29
    • Cabral, F.1
  • 7
    • 0035060238 scopus 로고    scopus 로고
    • Factors determining cellular mechanisms of resistance to antimitotic drugs
    • Cabral F. 2001. Factors determining cellular mechanisms of resistance to antimitotic drugs. Drug Resistance Updates 3:1-6.
    • (2001) Drug Resistance Updates , vol.3 , pp. 1-6
    • Cabral, F.1
  • 9
    • 0018236551 scopus 로고
    • The determination of similarities in amino acid composition among proteins separated by two-dimensional gel electrophoresis
    • Cabral F, Gottesman MM. 1978. The determination of similarities in amino acid composition among proteins separated by two-dimensional gel electrophoresis. Anal Biochem 91:548-556.
    • (1978) Anal Biochem , vol.91 , pp. 548-556
    • Cabral, F.1    Gottesman, M.M.2
  • 10
    • 0018370845 scopus 로고
    • High resoultion one- and two-dimensional electrophoretic analysis of mitochondrial membrane proteins
    • Cabral F, Schatz G. 1979. High resoultion one- and two-dimensional electrophoretic analysis of mitochondrial membrane proteins. Methods Enzymol 56:602-613.
    • (1979) Methods Enzymol , vol.56 , pp. 602-613
    • Cabral, F.1    Schatz, G.2
  • 11
    • 0018881050 scopus 로고
    • CHO mutants resistant to colchicine, colcemid or griseofulvin have an altered β-tubulin
    • Cabral F, Sobel ME, Gottesman MM. 1980. CHO mutants resistant to colchicine, colcemid or griseofulvin have an altered β-tubulin. Cell 20:29-36.
    • (1980) Cell , vol.20 , pp. 29-36
    • Cabral, F.1    Sobel, M.E.2    Gottesman, M.M.3
  • 12
    • 0020632261 scopus 로고
    • Taxol-requiring mutant of Chinese hamster ovary cells with impaired mitotic spindle assembly
    • Cabral F, Wible L, Brenner S, Brinkley BR. 1983. Taxol-requiring mutant of Chinese hamster ovary cells with impaired mitotic spindle assembly. J Cell Biol 97:30-39.
    • (1983) J Cell Biol , vol.97 , pp. 30-39
    • Cabral, F.1    Wible, L.2    Brenner, S.3    Brinkley, B.R.4
  • 13
    • 0022557228 scopus 로고
    • A mechanism of cellular resistance to drugs that interfere with microtubule assembly
    • Cabral F, Brady RC, Schibler MJ. 1986. A mechanism of cellular resistance to drugs that interfere with microtubule assembly. Ann N Y Acad Sci 466:745-756.
    • (1986) Ann N Y Acad Sci , vol.466 , pp. 745-756
    • Cabral, F.1    Brady, R.C.2    Schibler, M.J.3
  • 15
    • 77957374075 scopus 로고    scopus 로고
    • Microtubule-binding agents: A dynamic field of cancer therapeutics
    • Dumontet C, Jordan MA. 2010. Microtubule-binding agents: A dynamic field of cancer therapeutics. Nat Rev Drug Discov 9:790-803.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 790-803
    • Dumontet, C.1    Jordan, M.A.2
  • 16
    • 0022003642 scopus 로고
    • Differential expression of three α-tubulin genes in Chinese hamster ovary cells
    • Elliott EM, Okayama H, Sarangi F, Henderson G, Ling V. 1985. Differential expression of three α-tubulin genes in Chinese hamster ovary cells. Mol Cell Biol 5:236-241.
    • (1985) Mol Cell Biol , vol.5 , pp. 236-241
    • Elliott, E.M.1    Okayama, H.2    Sarangi, F.3    Henderson, G.4    Ling, V.5
  • 17
    • 0022622632 scopus 로고
    • Complete sequence of three α-tubulin cDNAs in Chinese hamster ovary cells: Each encodes a distinct α-tubulin isoprotein
    • Elliott EM, Henderson G, Sarangi F, Ling V. 1986. Complete sequence of three α-tubulin cDNAs in Chinese hamster ovary cells: Each encodes a distinct α-tubulin isoprotein. Mol Cell Biol 6:906-913.
    • (1986) Mol Cell Biol , vol.6 , pp. 906-913
    • Elliott, E.M.1    Henderson, G.2    Sarangi, F.3    Ling, V.4
  • 19
    • 79960654509 scopus 로고    scopus 로고
    • New insights into mechanisms of resistance to microtubule inhibitors
    • Ganguly A, Cabral F. 2011. New insights into mechanisms of resistance to microtubule inhibitors. Biochim Biophys Acta 1816:164-171.
    • (2011) Biochim Biophys Acta , vol.1816 , pp. 164-171
    • Ganguly, A.1    Cabral, F.2
  • 20
    • 78649660076 scopus 로고    scopus 로고
    • Paclitaxel dependent cell lines reveal a novel drug activity
    • Ganguly A, Yang H, Cabral F. 2010. Paclitaxel dependent cell lines reveal a novel drug activity. Mol Cancer Ther 9:2914-2923.
    • (2010) Mol Cancer Ther , vol.9 , pp. 2914-2923
    • Ganguly, A.1    Yang, H.2    Cabral, F.3
  • 21
    • 79958725353 scopus 로고    scopus 로고
    • Overexpression of mitotic centromere-associated kinesin stimulates microtubule detachment and confers resistance to paclitaxel
    • Ganguly A, Yang H, Cabral F. 2011. Overexpression of mitotic centromere-associated kinesin stimulates microtubule detachment and confers resistance to paclitaxel. Mol Cancer Ther 10:929-937.
    • (2011) Mol Cancer Ther , vol.10 , pp. 929-937
    • Ganguly, A.1    Yang, H.2    Cabral, F.3
  • 22
    • 0030758777 scopus 로고    scopus 로고
    • Paclitaxel-resistant human ovarian cancer cells have mutant β-tubulins that exhibit impaired paclitaxel-driven polymerization
    • Giannakakou P, Sackett DL, Kang Y-K, Zhan Z, Buters JTM, Fojo T, Poruchynsky MS. 1997. Paclitaxel-resistant human ovarian cancer cells have mutant β-tubulins that exhibit impaired paclitaxel-driven polymerization. J Biol Chem 272:17118-17125.
    • (1997) J Biol Chem , vol.272 , pp. 17118-17125
    • Giannakakou, P.1    Sackett, D.L.2    Kang, Y.-K.3    Zhan, Z.4    Buters, J.T.M.5    Fojo, T.6    Poruchynsky, M.S.7
  • 24
    • 0033588254 scopus 로고    scopus 로고
    • A β-tubulin leucine cluster involved in microtubule assembly and paclitaxel resistance
    • Gonzalez-Garay ML, Chang L, Blade K, Menick DR, Cabral F. 1999. A β-tubulin leucine cluster involved in microtubule assembly and paclitaxel resistance. J Biol Chem 274:23875-23882.
    • (1999) J Biol Chem , vol.274 , pp. 23875-23882
    • Gonzalez-Garay, M.L.1    Chang, L.2    Blade, K.3    Menick, D.R.4    Cabral, F.5
  • 25
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen M, Bujard H. 1992. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc Natl Acad Sci USA 89:5547-5551.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 26
    • 2142744812 scopus 로고    scopus 로고
    • Mutations in α- and β-tubulin that stabilize microtubules and confer resistance to colcemid and vinblastine
    • Hari M, Wang Y, Veeraraghavan S, Cabral F. 2003. Mutations in α- and β-tubulin that stabilize microtubules and confer resistance to colcemid and vinblastine. Mol Cancer Ther 2:597-605.
    • (2003) Mol Cancer Ther , vol.2 , pp. 597-605
    • Hari, M.1    Wang, Y.2    Veeraraghavan, S.3    Cabral, F.4
  • 27
    • 49649097047 scopus 로고    scopus 로고
    • The roles of beta-tubulin mutations and isotype expression in acquired drug resistance
    • Huzil JT, Chen K, Kurgan L, Tuszynski JA. 2007. The roles of beta-tubulin mutations and isotype expression in acquired drug resistance. Cancer Inform 3:159-181.
    • (2007) Cancer Inform , vol.3 , pp. 159-181
    • Huzil, J.T.1    Chen, K.2    Kurgan, L.3    Tuszynski, J.A.4
  • 28
    • 81855196008 scopus 로고    scopus 로고
    • Post-translational regulation of the microtubule cytoskeleton: Mechanisms and functions
    • Janke C, Bulinski JC. 2011. Post-translational regulation of the microtubule cytoskeleton: Mechanisms and functions. Nat Rev Mol Cell Biol 12:773-786.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 773-786
    • Janke, C.1    Bulinski, J.C.2
  • 30
    • 1942438028 scopus 로고    scopus 로고
    • Microtubules as a target for anticancer drugs
    • Jordan MA, Wilson L. 2004. Microtubules as a target for anticancer drugs. Nat Rev 4:253-265.
    • (2004) Nat Rev , vol.4 , pp. 253-265
    • Jordan, M.A.1    Wilson, L.2
  • 31
    • 80051599729 scopus 로고    scopus 로고
    • Peloruside- and laulimalide-resistant human ovarian carcinoma cells have betaI-tubulin mutations and altered expression of betaII- and betaIII-tubulin isotypes
    • Kanakkanthara A, Wilmes A, O'Brate A, Escuin D, Chan A, Gjyrezi A, Crawford J, Rawson P, Kivell B, Northcote PT, et al. 2011. Peloruside- and laulimalide-resistant human ovarian carcinoma cells have betaI-tubulin mutations and altered expression of betaII- and betaIII-tubulin isotypes. Mol Cancer Ther 10:1419-1429.
    • (2011) Mol Cancer Ther , vol.10 , pp. 1419-1429
    • Kanakkanthara, A.1    Wilmes, A.2    O'Brate, A.3    Escuin, D.4    Chan, A.5    Gjyrezi, A.6    Crawford, J.7    Rawson, P.8    Kivell, B.9    Northcote, P.T.10
  • 33
    • 77954505218 scopus 로고    scopus 로고
    • TUBA1A mutations cause wide spectrum lissencephaly (smooth brain) and suggest that multiple neuronal migration pathways converge on alpha tubulins
    • Kumar RA, Pilz DT, Babatz TD, Cushion TD, Harvey K, Topf M, Yates L, Robb S, Uyanik G, Mancini GMS, et al. 2010. TUBA1A mutations cause wide spectrum lissencephaly (smooth brain) and suggest that multiple neuronal migration pathways converge on alpha tubulins. Hum Mol Gen 19:2817-2827.
    • (2010) Hum Mol Gen , vol.19 , pp. 2817-2827
    • Kumar, R.A.1    Pilz, D.T.2    Babatz, T.D.3    Cushion, T.D.4    Harvey, K.5    Topf, M.6    Yates, L.7    Robb, S.8    Uyanik, G.9    Mancini, G.M.S.10
  • 34
    • 0025678371 scopus 로고
    • Cell line-specific differences in the control of cell cycle progression in the absence of mitosis
    • Kung AL, Sherwood SW, Schimke RT. 1990. Cell line-specific differences in the control of cell cycle progression in the absence of mitosis. Proc Natl Acad Sci USA 87:9553-9557.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9553-9557
    • Kung, A.L.1    Sherwood, S.W.2    Schimke, R.T.3
  • 36
    • 0023389780 scopus 로고
    • Identification of an acetylation site of Chlamydomonas α-tubulin
    • LeDizet M, Piperno G. 1987. Identification of an acetylation site of Chlamydomonas α-tubulin. Proc Natl Acad Sci USA 84:5720-5724.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5720-5724
    • LeDizet, M.1    Piperno, G.2
  • 39
    • 0037444386 scopus 로고    scopus 로고
    • Elevated levels of microtubule destabilizing factors in a taxol-resistant/dependent A549 cell line with an α-tubulin mutation
    • Martello LA, Verdier-Pinard P, Shen H-J, He L, Torres K, Orr GA, Horwitz SB. 2003. Elevated levels of microtubule destabilizing factors in a taxol-resistant/dependent A549 cell line with an α-tubulin mutation. Cancer Res 63:1207-1213.
    • (2003) Cancer Res , vol.63 , pp. 1207-1213
    • Martello, L.A.1    Verdier-Pinard, P.2    Shen, H.-J.3    He, L.4    Torres, K.5    Orr, G.A.6    Horwitz, S.B.7
  • 40
    • 0025872827 scopus 로고
    • Resistance to antimitotic drugs in Chinese hamster ovary cells correlates with changes in the level of polymerized tubulin
    • Minotti AM, Barlow SB, Cabral F. 1991. Resistance to antimitotic drugs in Chinese hamster ovary cells correlates with changes in the level of polymerized tubulin. J Biol Chem 266:3987-3994.
    • (1991) J Biol Chem , vol.266 , pp. 3987-3994
    • Minotti, A.M.1    Barlow, S.B.2    Cabral, F.3
  • 41
    • 0021686169 scopus 로고
    • Dynamic instability of microtubules
    • Mitchison T, Kirschner MW. 1984. Dynamic instability of microtubules. Nature 312:237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.W.2
  • 43
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales E, Wolf SG, Downing KH. 1998. Structure of the αβ tubulin dimer by electron crystallography. Nature 391:199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 45
    • 0023293040 scopus 로고
    • Microtubules containing acetylated alpha tubulin in mammalian cells in culture
    • Piperno G, LeDizet M, Chang X. 1987. Microtubules containing acetylated alpha tubulin in mammalian cells in culture. J Cell Biol 104:289-302.
    • (1987) J Cell Biol , vol.104 , pp. 289-302
    • Piperno, G.1    LeDizet, M.2    Chang, X.3
  • 48
    • 7444224866 scopus 로고    scopus 로고
    • Tumor cells resistant to a microtubule-depolymerizing hemiasterlin analogue, HTI-286, have mutations in alpha- or beta-tubulin and increased microtubule stability
    • Poruchynsky MS, Kim JH, Nogales E, Annable T, Loganzo F, Greenberger LM, Sackett DL, Fojo T. 2004. Tumor cells resistant to a microtubule-depolymerizing hemiasterlin analogue, HTI-286, have mutations in alpha- or beta-tubulin and increased microtubule stability. Biochemistry 43:13944-13954.
    • (2004) Biochemistry , vol.43 , pp. 13944-13954
    • Poruchynsky, M.S.1    Kim, J.H.2    Nogales, E.3    Annable, T.4    Loganzo, F.5    Greenberger, L.M.6    Sackett, D.L.7    Fojo, T.8
  • 49
    • 0022552877 scopus 로고
    • Taxol-dependent mutants of Chinese hamster ovary cells with alterations in α- and β-tubulin
    • Schibler M, Cabral F. 1986. Taxol-dependent mutants of Chinese hamster ovary cells with alterations in α- and β-tubulin. J Cell Biol 102:1522-1531.
    • (1986) J Cell Biol , vol.102 , pp. 1522-1531
    • Schibler, M.1    Cabral, F.2
  • 50
    • 0018114236 scopus 로고
    • Identification of a gene for β-tubulin in Aspergillus nidulans
    • Sheir-Neiss G, Lai MH, Morris NR. 1978. Identification of a gene for β-tubulin in Aspergillus nidulans. Cell 15:639-647.
    • (1978) Cell , vol.15 , pp. 639-647
    • Sheir-Neiss, G.1    Lai, M.H.2    Morris, N.R.3
  • 51
    • 0022408888 scopus 로고
    • Isolation and characterization of mutations in the beta-tubulin gene of Saccharomyces cerevisiae
    • Thomas JH, Neff NF, Botstein D. 1985. Isolation and characterization of mutations in the beta-tubulin gene of Saccharomyces cerevisiae. Genetics 112:715-734.
    • (1985) Genetics , vol.112 , pp. 715-734
    • Thomas, J.H.1    Neff, N.F.2    Botstein, D.3
  • 52
    • 79957626260 scopus 로고    scopus 로고
    • Phenotypic spectrum of the tubulin-related disorders and functional implications of disease-causing mutations
    • Tischfield MA, Cederquist GY, Gupta MLJ, Engle EC. 2011. Phenotypic spectrum of the tubulin-related disorders and functional implications of disease-causing mutations. Curr Opin Genet Dev 21:286-294.
    • (2011) Curr Opin Genet Dev , vol.21 , pp. 286-294
    • Tischfield, M.A.1    Cederquist, G.Y.2    Gupta, M.L.J.3    Engle, E.C.4
  • 53
    • 30144436015 scopus 로고    scopus 로고
    • Mutations at Leucine 215 of β-tubulin affect paclitaxel sensitivity by two distinct mechanisms
    • Wang Y, Yin S, Blade K, Cooper G, Menick DR, Cabral F. 2006. Mutations at Leucine 215 of β-tubulin affect paclitaxel sensitivity by two distinct mechanisms. Biochemistry 45:185-194.
    • (2006) Biochemistry , vol.45 , pp. 185-194
    • Wang, Y.1    Yin, S.2    Blade, K.3    Cooper, G.4    Menick, D.R.5    Cabral, F.6
  • 54
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann S, Weber K. 2003. Post-translational modifications regulate microtubule function. Nat Rev Mol Cell Biol 4:938-947.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 55
    • 77957793033 scopus 로고    scopus 로고
    • Inhibition of cell migration and cell division correlates with distinct effects of microtubule inhibiting drugs
    • Yang H, Ganguly A, Cabral F. 2010. Inhibition of cell migration and cell division correlates with distinct effects of microtubule inhibiting drugs. J Biol Chem 285:32242-32250.
    • (2010) J Biol Chem , vol.285 , pp. 32242-32250
    • Yang, H.1    Ganguly, A.2    Cabral, F.3
  • 56
    • 76649138611 scopus 로고    scopus 로고
    • Human mutations that confer paclitaxel resistance
    • Yin S, Bhattacharya R, Cabral F. 2010. Human mutations that confer paclitaxel resistance. Mol Cancer Ther 9:327-335.
    • (2010) Mol Cancer Ther , vol.9 , pp. 327-335
    • Yin, S.1    Bhattacharya, R.2    Cabral, F.3
  • 57
    • 84867858942 scopus 로고    scopus 로고
    • Random mutagenesis of β-tubulin defines a set of dispersed mutations that confer paclitaxel resistance
    • Yin S, Zeng C, Hari M, Cabral F. 2012. Random mutagenesis of β-tubulin defines a set of dispersed mutations that confer paclitaxel resistance. Pharm Res 29:2994-3006.
    • (2012) Pharm Res , vol.29 , pp. 2994-3006
    • Yin, S.1    Zeng, C.2    Hari, M.3    Cabral, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.