메뉴 건너뛰기




Volumn 17, Issue 3, 1998, Pages 658-666

Essential role of tubulin-folding cofactor D in microtubule assembly and its association with microtubules in fission yeast

Author keywords

Cofactor D; Fission yeast; MAPs; Microtubules; Polarity

Indexed keywords

FUNGAL PROTEIN; MICROTUBULE ASSOCIATED PROTEIN; PACLITAXEL; TUBULIN;

EID: 0032472940     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.3.658     Document Type: Article
Times cited : (73)

References (56)
  • 1
    • 0022726822 scopus 로고
    • Differential expression of essential and nonessential α-tubulin genes in Schizosaccharomyces pombe
    • Adachi, Y., Toda, T. and Yanagida, M. (1986) Differential expression of essential and nonessential α-tubulin genes in Schizosaccharomyces pombe. Mol. Cell. Biol., 6, 2168-2178.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2168-2178
    • Adachi, Y.1    Toda, T.2    Yanagida, M.3
  • 2
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, D.C. (1973) Principles that govern the folding of protein chains. Science, 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, D.C.1
  • 3
    • 0029164636 scopus 로고
    • Rlb2p, a yeast protein that binds to β-tubulin and participates in microtubule function in vivo
    • Archer, J.E., Vega, L.R. and Solomon, F. (1995) Rlb2p, a yeast protein that binds to β-tubulin and participates in microtubule function in vivo. Cell, 82, 425-434.
    • (1995) Cell , vol.82 , pp. 425-434
    • Archer, J.E.1    Vega, L.R.2    Solomon, F.3
  • 4
    • 0020410160 scopus 로고
    • Construction of Schizosaccharomyces pombe gene bank in a yeast bacterial shuttle vector and its use to isolate genes by complementation
    • Beach, D., Piper, M. and Nurse, P. (1982) Construction of Schizosaccharomyces pombe gene bank in a yeast bacterial shuttle vector and its use to isolate genes by complementation. Mol. Gen. Genet., 187, 326-329.
    • (1982) Mol. Gen. Genet. , vol.187 , pp. 326-329
    • Beach, D.1    Piper, M.2    Nurse, P.3
  • 5
    • 0030560763 scopus 로고    scopus 로고
    • Growing up in a dangerous environment: A network of multiple targeting and folding pathways for nascent polypeptides in the cytosol
    • Bukau, B., Hesterkamp, T. and Luirink, J. (1996) Growing up in a dangerous environment: a network of multiple targeting and folding pathways for nascent polypeptides in the cytosol. Trends Cell Biol., 6, 480-486.
    • (1996) Trends Cell Biol. , vol.6 , pp. 480-486
    • Bukau, B.1    Hesterkamp, T.2    Luirink, J.3
  • 6
    • 0024582786 scopus 로고
    • Dominant effects of tubulin overexpression in Saccharomyces cerevisiae
    • Burke, D., Gasdaska, P. and Hartwell, L. (1989) Dominant effects of tubulin overexpression in Saccharomyces cerevisiae. Mol. Cell. Biol., 9, 1049-1059.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1049-1059
    • Burke, D.1    Gasdaska, P.2    Hartwell, L.3
  • 7
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie, M., Tu, Y., Euskirchen, G., Ward, W.W. and Prasher, D.C. (1993) Green fluorescent protein as a marker for gene expression. Science, 263, 802-805.
    • (1993) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 8
    • 0027077442 scopus 로고
    • Function of protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
    • Frydman, J., Nimmesgern, E., Erdjument-Bromage, H., Wall, J.S., Tempst, P. and Hartl, F.-U. (1992) Function of protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J., 11, 4767-4778.
    • (1992) EMBO J. , vol.11 , pp. 4767-4778
    • Frydman, J.1    Nimmesgern, E.2    Erdjument-Bromage, H.3    Wall, J.S.4    Tempst, P.5    Hartl, F.-U.6
  • 9
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes β-actin folding
    • Gao, Y., Thomas, J.O., Chow, R.L., Lee, G.H. and Cowan, N.J. (1992) A cytoplasmic chaperonin that catalyzes β-actin folding. Cell, 69, 1043-1050.
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 10
    • 0027528871 scopus 로고
    • Two cofactors and cytoplasmic chaperonin are required for the folding of α- and β-tubulin
    • Gao, Y., Vainberg, I.E., Chow, R.L. and Cowan, N.J. (1993) Two cofactors and cytoplasmic chaperonin are required for the folding of α-and β-tubulin. Mol. Cell. Biol., 13, 2478-2485.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2478-2485
    • Gao, Y.1    Vainberg, I.E.2    Chow, R.L.3    Cowan, N.J.4
  • 12
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman, S., Wickner, S. and Maurizi, M. (1997) Protein quality control: triage by chaperones and proteases. Genes Dev., 11, 815-823.
    • (1997) Genes Dev. , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.3
  • 13
    • 0024215989 scopus 로고
    • Genetic engineering of Schizosaccharomyces pombe: A system for gene disruption and replacement using the ura4 gene as a selectable marker
    • Grimm, C., Kohli, J., Murray, J. and Maundrell, K. (1988) Genetic engineering of Schizosaccharomyces pombe: a system for gene disruption and replacement using the ura4 gene as a selectable marker. Mol. Gen. Genet., 215, 81-86.
    • (1988) Mol. Gen. Genet. , vol.215 , pp. 81-86
    • Grimm, C.1    Kohli, J.2    Murray, J.3    Maundrell, K.4
  • 14
    • 18744423994 scopus 로고
    • The use of cell division cycle mutants to investigate the control of microtubule distribution in the fission yeast
    • Hagan, I.M. and Hyams, J.S. (1988) The use of cell division cycle mutants to investigate the control of microtubule distribution in the fission yeast. J. Cell Sci., 89, 343-357.
    • (1988) J. Cell Sci. , vol.89 , pp. 343-357
    • Hagan, I.M.1    Hyams, J.S.2
  • 15
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996) Molecular chaperones in cellular protein folding. Nature, 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 16
    • 0021716157 scopus 로고
    • The NDA3 gene of fission yeast encodes β-tubulin: A cold-sensitive nda3 mutation reversibly blocks spindle formation and chromosome movement in mitosis
    • Hiraoka, Y., Toda, T. and Yanagida, M. (1984) The NDA3 gene of fission yeast encodes β-tubulin: a cold-sensitive nda3 mutation reversibly blocks spindle formation and chromosome movement in mitosis. Cell, 39, 349-358.
    • (1984) Cell , vol.39 , pp. 349-358
    • Hiraoka, Y.1    Toda, T.2    Yanagida, M.3
  • 17
    • 0028118917 scopus 로고
    • Microtubule organization and dynamics dependent on microtubule-associated proteins
    • Hirokawa, N. (1994) Microtubule organization and dynamics dependent on microtubule-associated proteins. Curr. Opin. Cell Biol., 6, 74-81.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 74-81
    • Hirokawa, N.1
  • 18
    • 0025741699 scopus 로고
    • The fission yeast γ-tubulin is essential for mitosis and is localized at microtubule organizing centers
    • Horio, T., Uzawa, S., Jung, M.K., Oakley, B.R., Tanaka, K. and Yanagida, M. (1991) The fission yeast γ-tubulin is essential for mitosis and is localized at microtubule organizing centers. J. Cell Sci., 99, 693-700.
    • (1991) J. Cell Sci. , vol.99 , pp. 693-700
    • Horio, T.1    Uzawa, S.2    Jung, M.K.3    Oakley, B.R.4    Tanaka, K.5    Yanagida, M.6
  • 19
    • 0025174216 scopus 로고
    • Chromosome instability mutants of Saccharomyces cerevisiae that are defective in microtubule-mediated processes
    • Hoyt, A.M., Stearns, T. and Botstein, D. (1990) Chromosome instability mutants of Saccharomyces cerevisiae that are defective in microtubule-mediated processes. Mol. Cell. Biol., 10, 223-234.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 223-234
    • Hoyt, A.M.1    Stearns, T.2    Botstein, D.3
  • 20
    • 0030748745 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability
    • Hoyt, M.A., Macke, J.P., Roberts, B.T. and Geiser, J.R. (1997) Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability. Genetics, 146, 849-857.
    • (1997) Genetics , vol.146 , pp. 849-857
    • Hoyt, M.A.1    Macke, J.P.2    Roberts, B.T.3    Geiser, J.R.4
  • 21
    • 0030059247 scopus 로고    scopus 로고
    • Morphogenetic properties of microtubules and mitotic spindle assembly
    • Hyman, A. and Karsenti, E. (1996) Morphogenetic properties of microtubules and mitotic spindle assembly. Cell, 84, 401-410.
    • (1996) Cell , vol.84 , pp. 401-410
    • Hyman, A.1    Karsenti, E.2
  • 22
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali
    • Ito, H., Fukuda, Y., Murata, K. and Kimura, A. (1983) Transformation of intact yeast cells treated with alkali. J. Bacteriol., 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 23
    • 0030809270 scopus 로고    scopus 로고
    • Protein folding in vivo: Unraveling complex pathways
    • Johnson, J.L. and Craig, E.A. (1997) Protein folding in vivo: unraveling complex pathways. Cell, 90, 201-204.
    • (1997) Cell , vol.90 , pp. 201-204
    • Johnson, J.L.1    Craig, E.A.2
  • 24
    • 0001665104 scopus 로고
    • Regulation of tubulin levels and microtubule asssembly in Saccharomyces cerevisiae: Consequence of altered tubulin gene copy number in yeast
    • Katz, J., Lenk, E. and Solomon, F. (1990) Regulation of tubulin levels and microtubule asssembly in Saccharomyces cerevisiae: consequence of altered tubulin gene copy number in yeast. Mol. Cell. Biol., 10, 2730-2736.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2730-2736
    • Katz, J.1    Lenk, E.2    Solomon, F.3
  • 25
    • 0027551389 scopus 로고
    • Non-motor microtubule-associated proteins
    • Lee, G. (1993) Non-motor microtubule-associated proteins. Curr. Opin. Cell Biol., 5, 88-94.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 88-94
    • Lee, G.1
  • 26
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • Liang, P. and MacRae, T.H. (1997) Molecular chaperones and the cytoskeleton. J. Cell Sci., 110, 1431-1440.
    • (1997) J. Cell Sci. , vol.110 , pp. 1431-1440
    • Liang, P.1    MacRae, T.H.2
  • 27
    • 0028945057 scopus 로고
    • Microtubules and microtubule-associated proteins
    • Mandelkow, E. and Mandelkow, E.-M. (1995) Microtubules and microtubule-associated proteins. Curr. Opin. Cell Biol., 7, 72-81.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 72-81
    • Mandelkow, E.1    Mandelkow, E.-M.2
  • 28
    • 0022825235 scopus 로고
    • Growth polarity and cytokinesis in fission yeast: The role of the cytoskeleton
    • Marks, J.H., Hagan, I.M. and Hyams, J.S. (1986) Growth polarity and cytokinesis in fission yeast: the role of the cytoskeleton. J. Cell Sci. Suppl., 5, 229-241.
    • (1986) J. Cell Sci. Suppl. , vol.5 , pp. 229-241
    • Marks, J.H.1    Hagan, I.M.2    Hyams, J.S.3
  • 29
    • 0023663429 scopus 로고
    • The role of tubulin polymerization during spindle elongation
    • Masuda, H. and Cande, W.Z. (1987) The role of tubulin polymerization during spindle elongation. Cell, 49, 193-202.
    • (1987) Cell , vol.49 , pp. 193-202
    • Masuda, H.1    Cande, W.Z.2
  • 30
    • 0030773728 scopus 로고    scopus 로고
    • Tea1p and the microtubular cytoskeleton are important for generating global spatial order within the fission yeast cell
    • Mata, F. and Nurse, P. (1997) tea1p and the microtubular cytoskeleton are important for generating global spatial order within the fission yeast cell. Cell, 89, 939-949.
    • (1997) Cell , vol.89 , pp. 939-949
    • Mata, F.1    Nurse, P.2
  • 31
    • 0024095920 scopus 로고
    • Truncation of the carboxy-terminal domain of yeast β-tubulin causes temperature-sensitive growth and hypersensitivity to antimitotic drugs
    • Matsuzaki, F., Matsumoto, S. and Yahara, I. (1988) Truncation of the carboxy-terminal domain of yeast β-tubulin causes temperature-sensitive growth and hypersensitivity to antimitotic drugs. J. Cell Biol. 107, 1427-1435.
    • (1988) J. Cell Biol. , vol.107 , pp. 1427-1435
    • Matsuzaki, F.1    Matsumoto, S.2    Yahara, I.3
  • 32
    • 0025298571 scopus 로고
    • Nmt1 of fission yeast
    • Maundrell, K. (1990) nmt1 of fission yeast. J. Biol. Chem., 265, 10857-10864.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10857-10864
    • Maundrell, K.1
  • 33
    • 0027293897 scopus 로고
    • Chaperonin-mediated folding of vertebrate actin-related protein and γ-tubulin
    • Melki, R., Vainberg, I.E., Chow, R.L. and Cowan, N.J. (1993) Chaperonin-mediated folding of vertebrate actin-related protein and γ-tubulin. J. Cell Biol., 122, 1301-1310.
    • (1993) J. Cell Biol. , vol.122 , pp. 1301-1310
    • Melki, R.1    Vainberg, I.E.2    Chow, R.L.3    Cowan, N.J.4
  • 34
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison, T. and Kirschner, M.W. (1984) Dynamic instability of microtubule growth. Nature, 31, 237-242.
    • (1984) Nature , vol.31 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.W.2
  • 35
    • 0022919318 scopus 로고
    • Beyond self-assembly: From microtubules to morphogenesis
    • Mitchison, T. and Kirschner, M.W. (1986) Beyond self-assembly: from microtubules to morphogenesis. Cell, 45, 329-342.
    • (1986) Cell , vol.45 , pp. 329-342
    • Mitchison, T.1    Kirschner, M.W.2
  • 36
    • 0022042267 scopus 로고
    • Growth in cell length in the fission yeast Schizosaccharomyces pombe
    • Mitchison, J.M. and Nurse, P. (1985) Growth in cell length in the fission yeast Schizosaccharomyces pombe. J. Cell Sci., 75, 357-376.
    • (1985) J. Cell Sci. , vol.75 , pp. 357-376
    • Mitchison, J.M.1    Nurse, P.2
  • 37
    • 0020600632 scopus 로고
    • Isolation of the β-tubulin gene from yeast and demonstration of its essential function in vivo
    • Neff, N., Thomas, J.H., Grisafi, P. and Botstein, D. (1983) Isolation of the β-tubulin gene from yeast and demonstration of its essential function in vivo. Cell, 33, 211-219.
    • (1983) Cell , vol.33 , pp. 211-219
    • Neff, N.1    Thomas, J.H.2    Grisafi, P.3    Botstein, D.4
  • 38
    • 0017157413 scopus 로고
    • Genetic control of the cell division cycle in the fission yeast Schizosaccharomyces pombe
    • Nurse, P., Thuriaux, P. and Nasmyth, K. (1976) Genetic control of the cell division cycle in the fission yeast Schizosaccharomyces pombe. Mol. Gen. Genet., 146, 167-178.
    • (1976) Mol. Gen. Genet. , vol.146 , pp. 167-178
    • Nurse, P.1    Thuriaux, P.2    Nasmyth, K.3
  • 39
    • 0031106824 scopus 로고    scopus 로고
    • Molecular chaperones: Towards a characterization of the heat-shock protein 70 family
    • Rassow, J., von Ahsen, O., Bömer,U. and Pfanner, N. (1997) Molecular chaperones: towards a characterization of the heat-shock protein 70 family. Trends Cell Biol., 7, 129-133
    • (1997) Trends Cell Biol. , vol.7 , pp. 129-133
    • Rassow, J.1    Von Ahsen, O.2    Bömer, U.3    Pfanner, N.4
  • 41
    • 0029929297 scopus 로고    scopus 로고
    • CLIPs for organelle-microtubule interactions
    • Rickard, J.E. and Kreis, T.E. (1996) CLIPs for organelle-microtubule interactions. Trends Cell Biol., 6, 178-183.
    • (1996) Trends Cell Biol. , vol.6 , pp. 178-183
    • Rickard, J.E.1    Kreis, T.E.2
  • 43
    • 0022819847 scopus 로고
    • Genetically essential and nonessential α-tubulin genes specify functionally interchangeable proteins
    • Schatz, P.J., Solomon, F. and Botstein, D. (1986) Genetically essential and nonessential α-tubulin genes specify functionally interchangeable proteins. Mol. Cell. Biol., 6, 3722-2733.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3722-12733
    • Schatz, P.J.1    Solomon, F.2    Botstein, D.3
  • 44
    • 0029614344 scopus 로고    scopus 로고
    • A highly divergent γ-tubulin gene is essential for cell growth and proper microtubule organization in Saccharomyces cerevisiae
    • Sobel, S.G. and Snyder, M. (1996) A highly divergent γ-tubulin gene is essential for cell growth and proper microtubule organization in Saccharomyces cerevisiae. J. Cell Biol., 131, 1775-1788.
    • (1996) J. Cell Biol. , vol.131 , pp. 1775-1788
    • Sobel, S.G.1    Snyder, M.2
  • 45
    • 0025057481 scopus 로고
    • Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function
    • Stearns, T., Hoyt, M.A. and Botstein, D. (1990) Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function. Genetics, 124, 251-262.
    • (1990) Genetics , vol.124 , pp. 251-262
    • Stearns, T.1    Hoyt, M.A.2    Botstein, D.3
  • 47
    • 0028822679 scopus 로고
    • Quasi-native chaperonin-bound intermediates in facilitated protein folding
    • Tian, G., Vainberg, I.E., Tap, W.D., Lewis, S.A. and Cowan, N.J. (1995) Quasi-native chaperonin-bound intermediates in facilitated protein folding. J. Biol. Chem., 270, 23910-23913.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23910-23913
    • Tian, G.1    Vainberg, I.E.2    Tap, W.D.3    Lewis, S.A.4    Cowan, N.J.5
  • 49
    • 0030820735 scopus 로고    scopus 로고
    • Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
    • Tian, G., Lewis, S.A., Feierbach, B., Stearns, T., Rommelaere, H., Ampe, C. and Cowan, N.J. (1997) Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors. J. Cell Biol., 138, 821-832.
    • (1997) J. Cell Biol. , vol.138 , pp. 821-832
    • Tian, G.1    Lewis, S.A.2    Feierbach, B.3    Stearns, T.4    Rommelaere, H.5    Ampe, C.6    Cowan, N.J.7
  • 50
    • 0021187647 scopus 로고
    • Identification of the pleiotropic cell cycle gene NDA2 as one of two different α-tubulin genes in Schizosaccharomyces pombe
    • Toda, T., Adachi, Y. Hiraoka, Y. and Yanagida, M. (1984) Identification of the pleiotropic cell cycle gene NDA2 as one of two different α-tubulin genes in Schizosaccharomyces pombe. Cell, 37, 233-242.
    • (1984) Cell , vol.37 , pp. 233-242
    • Toda, T.1    Adachi, Y.2    Hiraoka, Y.3    Yanagida, M.4
  • 51
    • 0029838558 scopus 로고    scopus 로고
    • + is required for establishment of growth polarity and functionally interacts with protein kinase C and an osmosensing MAP-kinase pathway
    • + is required for establishment of growth polarity and functionally interacts with protein kinase C and an osmosensing MAP-kinase pathway. J. Cell Sci., 109, 2331-2342.
    • (1996) J. Cell Sci. , vol.109 , pp. 2331-2342
    • Toda, T.1    Niwa, H.2    Nemoto, T.3    Dhut, S.4    Eddison, M.5    Yanagida, M.6    Hirata, D.7
  • 52
    • 0009543358 scopus 로고
    • Isolation of type I and II topoisomerase mutants from fission yeast: Single and double mutants show different phenotypes in cell growth and chromatin organization
    • Uemura, T. and Yanagida, M. (1984) Isolation of type I and II topoisomerase mutants from fission yeast: single and double mutants show different phenotypes in cell growth and chromatin organization. EMBO J., 3, 1737-1744.
    • (1984) EMBO J. , vol.3 , pp. 1737-1744
    • Uemura, T.1    Yanagida, M.2
  • 53
    • 0021051084 scopus 로고
    • Visualization of chromosomes in mitotically arrested cells of the fission yeast Schizosaccharomyces pombe
    • Umesono, K., Hiraoka, Y., Toda, T. and Yanagida, M. (1983a) Visualization of chromosomes in mitotically arrested cells of the fission yeast Schizosaccharomyces pombe. Curr. Genet., 7, 123-128.
    • (1983) Curr. Genet. , vol.7 , pp. 123-128
    • Umesono, K.1    Hiraoka, Y.2    Toda, T.3    Yanagida, M.4
  • 54
    • 0020551993 scopus 로고
    • Two cell division cycle genes NDA2 and NDA3 of the fission yeast Schizosaccharomyces pombe control microtubular organization and sensitivity of antimitotic benzimidazole compounds
    • Umesono, K., Toda, T., Hayashi, S. and Yanagida, M. (1983b) Two cell division cycle genes NDA2 and NDA3 of the fission yeast Schizosaccharomyces pombe control microtubular organization and sensitivity of antimitotic benzimidazole compounds. J. Mol. Biol., 168, 271-284.
    • (1983) J. Mol. Biol. , vol.168 , pp. 271-284
    • Umesono, K.1    Toda, T.2    Hayashi, S.3    Yanagida, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.