메뉴 건너뛰기




Volumn 112, Issue 23, 1999, Pages 4281-4289

Tubulin polyglutamylase: Isozymic variants and regulation during the cell cycle in HeLa cells

Author keywords

Cell cycle; Glutamylation; Microtubule; Mitosis; Polyglutamylation; Posttranslational modification; Tubulin

Indexed keywords

AMYLASE; DOCETAXEL; HYDROXYUREA; MICROTUBULE ASSOCIATED PROTEIN; NOCODAZOLE; POLYGLUTAMIC ACID; TUBULIN; TUBULIN POLYGLUTAMYLASE; UNCLASSIFIED DRUG;

EID: 0033491708     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (39)

References (41)
  • 3
    • 0027934789 scopus 로고
    • Developmental regulation of polyglutamylated alpha- and beta-tubulin in mouse brain neurons
    • Audebert, S., Koulakoff, A., Berwald-Netter, Y., Gros, F., Denoulet, P. and Eddé, B. (1994). Developmental regulation of polyglutamylated alpha- and beta-tubulin in mouse brain neurons. J. Cell Sci. 107, 2313.
    • (1994) J. Cell Sci. , vol.107 , pp. 2313
    • Audebert, S.1    Koulakoff, A.2    Berwald-Netter, Y.3    Gros, F.4    Denoulet, P.5    Eddé, B.6
  • 4
    • 0023829224 scopus 로고
    • A monoclonal antibody against the type II isotype of β-tubulin. Preparation of isotypically altered tubulin
    • Banerjee, A., Roach, M. C., Wall, K. A., Lopata, M. A., Cleveland, D. W. and Ludueña, R. F. (1988). A monoclonal antibody against the type II isotype of β-tubulin. Preparation of isotypically altered tubulin. J. Biol. Chem. 263, 3029.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3029
    • Banerjee, A.1    Roach, M.C.2    Wall, K.A.3    Lopata, M.A.4    Cleveland, D.W.5    Ludueña, R.F.6
  • 5
    • 0032517865 scopus 로고    scopus 로고
    • Centriole disassembly in vivo and its effect on centrosome structure and function in vertebrate cells
    • Bobinnec, Y., Khodjakov, A., Mir, L. M., Rieder, C. L., Eddé, B. and Bornens, M. (1998a). Centriole disassembly in vivo and its effect on centrosome structure and function in vertebrate cells. J. Cell Biol. 143, 1575.
    • (1998) J. Cell Biol. , vol.143 , pp. 1575
    • Bobinnec, Y.1    Khodjakov, A.2    Mir, L.M.3    Rieder, C.L.4    Eddé, B.5    Bornens, M.6
  • 7
    • 0028110393 scopus 로고
    • Polyglutamylation of tubulin as a progressive regulator of in vitro interaction between the microtubule-associated protein Tau and tubulin
    • Boucher, D., Larcher, J. C., Gros, F. and Denoulet, P. (1994). Polyglutamylation of tubulin as a progressive regulator of in vitro interaction between the microtubule-associated protein Tau and tubulin. Biochemistry 33, 12471.
    • (1994) Biochemistry , vol.33 , pp. 12471
    • Boucher, D.1    Larcher, J.C.2    Gros, F.3    Denoulet, P.4
  • 8
    • 0028210453 scopus 로고
    • Glutamylated tubulin probed in ciliates with the monoclonal antibody GT335
    • Bré, M. H., De Néchaud, B., Wolff, A. and Fleury, A. (1994), Glutamylated tubulin probed in ciliates with the monoclonal antibody GT335. Cell Motil. Cytoskel. 27, 337.
    • (1994) Cell Motil. Cytoskel. , vol.27 , pp. 337
    • Bré, M.H.1    De Néchaud, B.2    Wolff, A.3    Fleury, A.4
  • 9
    • 0033005733 scopus 로고    scopus 로고
    • Accessory protein regulation of microtubule dynamics throughout the cell cycle
    • Cassimeris, L. (1999). Accessory protein regulation of microtubule dynamics throughout the cell cycle. Curr. Opin. Cell Biol. 11, 134.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 134
    • Cassimeris, L.1
  • 10
    • 0023097820 scopus 로고
    • Mammalian folyl-gamma-polyglutamate synthetase. 2. Substrate specificity and kinetic properties
    • Cichowicz, D. J. and Shane, B. (1987). Mammalian folyl-gamma-polyglutamate synthetase. 2. Substrate specificity and kinetic properties. Biochemistry 26, 513.
    • (1987) Biochemistry , vol.26 , pp. 513
    • Cichowicz, D.J.1    Shane, B.2
  • 11
    • 0030009589 scopus 로고    scopus 로고
    • Tubulin post-translational modifications in the primitive protist Trichomonas vaginalis
    • Delgado-Viscogliosi, P., Brugerolle, G. and Viscogliosi, E. (1996). Tubulin post-translational modifications in the primitive protist Trichomonas vaginalis. Cell Motil. Cytoskel. 33, 288.
    • (1996) Cell Motil. Cytoskel. , vol.33 , pp. 288
    • Delgado-Viscogliosi, P.1    Brugerolle, G.2    Viscogliosi, E.3
  • 12
    • 0029964648 scopus 로고    scopus 로고
    • ATF/CREB site mediated transcriptional activation and p53 dependent repression of the cyclin A promoter
    • Desdouets, C., Ory, C., Matesic, G., Soussi, T., Brechot, C. and Sobczak, T. J. (1996). ATF/CREB site mediated transcriptional activation and p53 dependent repression of the cyclin A promoter. FEBS Lett. 385, 34.
    • (1996) FEBS Lett. , vol.385 , pp. 34
    • Desdouets, C.1    Ory, C.2    Matesic, G.3    Soussi, T.4    Brechot, C.5    Sobczak, T.J.6
  • 14
    • 0022894655 scopus 로고
    • Alpha-Carboxyl-linked glutamates in the folylpolyglutamates of Escherichia coli
    • Ferone, R., Hanlon, M. H., Singer, S. C. and Hunt, D. F. (1986a). alpha-Carboxyl-linked glutamates in the folylpolyglutamates of Escherichia coli. J. Biol. Chem. 261, 16356.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16356
    • Ferone, R.1    Hanlon, M.H.2    Singer, S.C.3    Hunt, D.F.4
  • 15
    • 0022869691 scopus 로고
    • In vitro synthesis of alpha-carboxyl-linked folylpolyglutamates by an enzyme preparation from Escherichia coli
    • Ferone, R., Singer, S. C. and Hunt, D. F. (1986b). In vitro synthesis of alpha-carboxyl-linked folylpolyglutamates by an enzyme preparation from Escherichia coli. J. Biol. Chem. 261, 16363.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16363
    • Ferone, R.1    Singer, S.C.2    Hunt, D.F.3
  • 19
    • 0029814394 scopus 로고    scopus 로고
    • Interaction of kinesin motor domains with alpha- and beta-tubulin subunits at a Tau-independant manner
    • Larcher, J. C., Boucher, D., Lazereg, S., Gros, F. and Denoulet, P. (1996). Interaction of kinesin motor domains with alpha- and beta-tubulin subunits at a Tau-independant manner. J. Biol. Chem. 271, 22117.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22117
    • Larcher, J.C.1    Boucher, D.2    Lazereg, S.3    Gros, F.4    Denoulet, P.5
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 21
    • 0022398355 scopus 로고
    • Three expressed sequences within the human β-tubulin multigene family each define a distinct isotype
    • Lewis, A. L., Gilmartin, M. E., Hall, J. L. and Cowan, N. J. (1985). Three expressed sequences within the human β-tubulin multigene family each define a distinct isotype. J. Mol. Biol. 182, 11.
    • (1985) J. Mol. Biol. , vol.182 , pp. 11
    • Lewis, A.L.1    Gilmartin, M.E.2    Hall, J.L.3    Cowan, N.J.4
  • 22
    • 0023662301 scopus 로고
    • Free intermingling of mammalian β-tubulin isotypes among functionally distinct microtubules
    • Lewis, S. A., Gu, W. and Cowan, N. J. (1987). Free intermingling of mammalian β-tubulin isotypes among functionally distinct microtubules. Cell 49, 539.
    • (1987) Cell , vol.49 , pp. 539
    • Lewis, S.A.1    Gu, W.2    Cowan, N.J.3
  • 23
    • 0028071995 scopus 로고
    • Class I and IVa beta-tubulin isotypes expressed in adult mouse brain are glutamylated
    • Mary, J., Redeker, V., Le Caer, J. P., Promé, J. C. and Rossier, J. (1994). Class I and IVa beta-tubulin isotypes expressed in adult mouse brain are glutamylated. FEBS Lett. 353, 89.
    • (1994) FEBS Lett. , vol.353 , pp. 89
    • Mary, J.1    Redeker, V.2    Le Caer, J.P.3    Promé, J.C.4    Rossier, J.5
  • 24
    • 0001968556 scopus 로고
    • Method of centrosome isolation from cultured animal cells
    • ed. J. E. Célis, San Diego: Academic Press
    • Moudjou, M. and Bornens, M. (1994). Method of centrosome isolation from cultured animal cells. In Cell Biology: A Library Handbook (ed. J. E. Célis), pp. 595. San Diego: Academic Press.
    • (1994) Cell Biology: A Library Handbook , pp. 595
    • Moudjou, M.1    Bornens, M.2
  • 25
    • 0030772842 scopus 로고    scopus 로고
    • Cold-adapted microtubules: Characterization of tubulin posttranslational modilications in the Antarctic ciliate Euplotes focardii
    • Pucciarelli, S., Ballarini, P. and Miceli, C. (1997). Cold-adapted microtubules: Characterization of tubulin posttranslational modilications in the Antarctic ciliate Euplotes focardii. Cell Motil. Cytoskel. 38, 329.
    • (1997) Cell Motil. Cytoskel. , vol.38 , pp. 329
    • Pucciarelli, S.1    Ballarini, P.2    Miceli, C.3
  • 26
    • 0031985608 scopus 로고    scopus 로고
    • Altered β-tubulin isotype expression in paclitaxel-resistant human prostate carcinoma cells
    • Ranganathan, S., Benetatos, C. A., Colarusso, P. J., Dexter, D. W. and Hudes, G. R. (1998). Altered β-tubulin isotype expression in paclitaxel-resistant human prostate carcinoma cells. Br. J. Cancel 77, 562.
    • (1998) Br. J. Cancel , vol.77 , pp. 562
    • Ranganathan, S.1    Benetatos, C.A.2    Colarusso, P.J.3    Dexter, D.W.4    Hudes, G.R.5
  • 27
    • 0026338717 scopus 로고
    • Structure of the polyglutamyl side chain posttranslationally added to α-tubulin
    • Redeker, V., Le Caer, J.-P., Rossier, J. and Promé, J.-C. (1991). Structure of the polyglutamyl side chain posttranslationally added to α-tubulin. J. Biol. Chem. 266, 23461.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23461
    • Redeker, V.1    Le Caer, J.-P.2    Rossier, J.3    Promé, J.-C.4
  • 28
    • 0026447041 scopus 로고
    • Structure of tubulin C-terminal domain obtained hy subtilisin treatment. The major α and β tubulin isotypes from pig brain are glutamylated
    • Redeker, V., Melki, R., Promé, J.-C., Le Caer, J.-P. and Rossier, J. (1992). Structure of tubulin C-terminal domain obtained hy subtilisin treatment. The major α and β tubulin isotypes from pig brain are glutamylated. FEBS Lett. 313, 185.
    • (1992) FEBS Lett. , vol.313 , pp. 185
    • Redeker, V.1    Melki, R.2    Promé, J.-C.3    Le Caer, J.-P.4    Rossier, J.5
  • 29
    • 0029800944 scopus 로고    scopus 로고
    • Structure of the C-terminal tail of α-tubulin: Increase of heterogeneity from newborn to adult
    • Redeker, V., Ruscuni, F., Mary, J., Promé, D. and Rossier, J. (1996). Structure of the C-terminal tail of α-tubulin: increase of heterogeneity from newborn to adult. J. Neurochem. 67, 2104.
    • (1996) J. Neurochem. , vol.67 , pp. 2104
    • Redeker, V.1    Ruscuni, F.2    Mary, J.3    Promé, D.4    Rossier, J.5
  • 30
    • 0032553017 scopus 로고    scopus 로고
    • Posttranslational moditications of the C terminus of alpha-tubulin in adult rat brain: Alpha 4 is glutamylated at two residues
    • Redeker, V., Rossier, J. and Frankfurter, A. (1998). Posttranslational moditications of the C terminus of alpha-tubulin in adult rat brain: alpha 4 is glutamylated at two residues. Biochemistry 37, 14838.
    • (1998) Biochemistry , vol.37 , pp. 14838
    • Redeker, V.1    Rossier, J.2    Frankfurter, A.3
  • 31
  • 32
    • 0028817534 scopus 로고
    • Characterization of post-translational modifications of brain tubulin ny matrix-assisted laser desorption/ionization mass spectrometry: Direct one-step analysis of a limited subtilisin digest
    • Rüdiger, A., Rüdiger, M., Weber, K. and Schomhurg, D. (1995). Characterization of post-translational modifications of brain tubulin ny matrix-assisted laser desorption/ionization mass spectrometry: direct one-step analysis of a limited subtilisin digest. Anal. Biochem. 224, 532.
    • (1995) Anal. Biochem. , vol.224 , pp. 532
    • Rüdiger, A.1    Rüdiger, M.2    Weber, K.3    Schomhurg, D.4
  • 33
    • 0026773956 scopus 로고
    • Class II tubulin, the major brain beta tubulin isotype is polyglutamylated on glutamic acid residue 435
    • Rüdiger, M., Plessman, U., Klöppel, K. D., Wehland, J. and Weber, K. (1992). Class II tubulin, the major brain beta tubulin isotype is polyglutamylated on glutamic acid residue 435. FEBS Lett. 308, 101.
    • (1992) FEBS Lett. , vol.308 , pp. 101
    • Rüdiger, M.1    Plessman, U.2    Klöppel, K.D.3    Wehland, J.4    Weber, K.5
  • 34
    • 0032537564 scopus 로고    scopus 로고
    • Posttranslational modifications of trichomonad tubulins: Identification of multiple glutamylation sites
    • Schneider, A., Plessmann, U., Felleisen, R. and Weber, K. (1998). Posttranslational modifications of trichomonad tubulins: identification of multiple glutamylation sites. FEBS Lett. 429, 399.
    • (1998) FEBS Lett. , vol.429 , pp. 399
    • Schneider, A.1    Plessmann, U.2    Felleisen, R.3    Weber, K.4
  • 35
    • 0030985055 scopus 로고    scopus 로고
    • Post-translational modifications and multiple tubulin isoforms in Nicotiana tabacum L. cells
    • Smertenko, A., Blume, Y., Viklicky, V., Opatrny, Z. and Draber, P. (1997). Post-translational modifications and multiple tubulin isoforms in Nicotiana tabacum L. cells. Planta 201, 349.
    • (1997) Planta , vol.201 , pp. 349
    • Smertenko, A.1    Blume, Y.2    Viklicky, V.3    Opatrny, Z.4    Draber, P.5
  • 36
    • 0011202760 scopus 로고
    • Identification of conserved isotype-defining variable region sequences for four vertebrate β tubulin polypeptide classes
    • Sullivan, K. F. and Cleveland, D. W. (1986). Identification of conserved isotype-defining variable region sequences for four vertebrate β tubulin polypeptide classes. Proc. Nat. Acad. Sci. USA 83, 4327.
    • (1986) Proc. Nat. Acad. Sci. USA , vol.83 , pp. 4327
    • Sullivan, K.F.1    Cleveland, D.W.2
  • 37
    • 0020031810 scopus 로고
    • A taxol-dependant procedure for the isolation of microtubules and microtubule-associated proteins (MAPs)
    • Vallee, R. V. (1982). A taxol-dependant procedure for the isolation of microtubules and microtubule-associated proteins (MAPs). J. Cell Biol. 92, 435.
    • (1982) J. Cell Biol. , vol.92 , pp. 435
    • Vallee, R.V.1
  • 38
    • 0032839187 scopus 로고    scopus 로고
    • Isolation of tubulin polyglutamylase from Crithidia; binding to microtubules and tubulin, and glutamylation of mammalian brain alpha- and beta-tubulins
    • Westermann, S., Schneider, A., Horn, E. K. and Weber, K. (1999). Isolation of tubulin polyglutamylase from Crithidia; binding to microtubules and tubulin, and glutamylation of mammalian brain alpha- and beta-tubulins. J. Cell Sci. 2185.
    • (1999) J. Cell Sci. , pp. 2185
    • Westermann, S.1    Schneider, A.2    Horn, E.K.3    Weber, K.4
  • 39
    • 0020266009 scopus 로고
    • High level of tubulin microheterogeneity in the mouse brain
    • Wolff, A., Denoulet, P. and Jeantet, C. (1982). High level of tubulin microheterogeneity in the mouse brain. Neurosci. Lett. 31, 323.
    • (1982) Neurosci. Lett. , vol.31 , pp. 323
    • Wolff, A.1    Denoulet, P.2    Jeantet, C.3
  • 41
    • 0028102231 scopus 로고
    • Structure of the polyglutamyl chain of tubulin: Occurrence of alpha and gamma linkages between glutamyl units revealed by monoreactive polyclonal antibodies
    • Wolff, A., Houdayer, M., Chillet, D., De Néchaud, B. and Denoulet, P. (1994). Structure of the polyglutamyl chain of tubulin: Occurrence of alpha and gamma linkages between glutamyl units revealed by monoreactive polyclonal antibodies. Biol. Cell 81, 11.
    • (1994) Biol. Cell , vol.81 , pp. 11
    • Wolff, A.1    Houdayer, M.2    Chillet, D.3    De Néchaud, B.4    Denoulet, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.