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Volumn 135, Issue 6, 1996, Pages 1525-1534

α-Tubulin limits its own synthesis: Evidence for a mechanism involving translational repression

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; COMPLEMENTARY DNA;

EID: 0030481488     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.135.6.1525     Document Type: Article
Times cited : (55)

References (32)
  • 1
    • 0028037828 scopus 로고
    • Stable expression of heterologous microtubule associated proteins in Chinese hamster ovary cells: Evidence for differing roles of MAPs in microtubule organization
    • Barlow, S.B., M.L. Gonzalez-Garay, R.R. West, J.B. Olmsted, and F. Cabral. 1994. Stable expression of heterologous microtubule associated proteins in Chinese hamster ovary cells: evidence for differing roles of MAPs in microtubule organization. J. Cell Biol. 126:1017-1029.
    • (1994) J. Cell Biol. , vol.126 , pp. 1017-1029
    • Barlow, S.B.1    Gonzalez-Garay, M.L.2    West, R.R.3    Olmsted, J.B.4    Cabral, F.5
  • 2
    • 0023391463 scopus 로고
    • Mutations affecting assembly and stability of tubulin: Evidence for a non-essential β-tubulin in CHO cells
    • Boggs, B., and F. Cabral. 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
  • 3
    • 0024582786 scopus 로고
    • Dominant effects of tubulin overexpression in Saccharomyces cerevisiae
    • Burke, D., P. Gasdaska, and L. Hartwell. 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
  • 4
    • 0018236551 scopus 로고
    • The determination of similarities in amino acid composition among proteins separated by two-dimensional gel electrophoresis
    • Cabrai, F., and M.M. Gottesman. 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
    • Cabrai, F.1    Gottesman, M.M.2
  • 5
    • 0018370845 scopus 로고
    • One- and two-dimensional electrophoretic analysis of mitochondrial membrane proteins
    • Cabrai, F., and G. Schatz. 1979. One-and two-dimensional electrophoretic analysis of mitochondrial membrane proteins. Methods Enzymol. 56:602-613.
    • (1979) Methods Enzymol. , vol.56 , pp. 602-613
    • Cabrai, F.1    Schatz, G.2
  • 6
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C., and H. Okayama. 1987. High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7:2745-2752.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 8
    • 0027178264 scopus 로고
    • Specific binding of human dihydrofolate reductase protein to dihydrofolate reductase messenger RNA in vitro
    • Chu, E., C.H. Takimoto, D. Voeller, J.L. Grem, and C.J. Allegra. 1993. Specific binding of human dihydrofolate reductase protein to dihydrofolate reductase messenger RNA in vitro. Biochemistry. 32:4756-4760.
    • (1993) Biochemistry , vol.32 , pp. 4756-4760
    • Chu, E.1    Takimoto, C.H.2    Voeller, D.3    Grem, J.L.4    Allegra, C.J.5
  • 9
    • 0024372769 scopus 로고
    • Autoregulated control of tubulin synthesis in animal cells
    • Cleveland, D.W. 1989. Autoregulated control of tubulin synthesis in animal cells. Curr. Opin. Cell Biol. 1:10-14.
    • (1989) Curr. Opin. Cell Biol. , vol.1 , pp. 10-14
    • Cleveland, D.W.1
  • 10
    • 0029115509 scopus 로고
    • Vinblastine suppresses dynamics of individual microtubules in living interphase cells
    • Dhamodharan, R., M.A. Jordan, D. Thrower, L. Wilson, and P. Wadsworth, 1995. Vinblastine suppresses dynamics of individual microtubules in living interphase cells. Mol. Biol. Cell. 6:1215-1229.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1215-1229
    • Dhamodharan, R.1    Jordan, M.A.2    Thrower, D.3    Wilson, L.4    Wadsworth, P.5
  • 11
    • 0022622632 scopus 로고
    • Complete sequence of three α-tubulin cDNAs in Chinese hamster ovary cells: Each encodes a distinct α-tubulin isoprotein
    • Elliott, E.M., G. Henderson, F. Sarangi, and V. Ling. 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
  • 12
    • 0029113391 scopus 로고
    • Overexpression of an epitopetagged β-tubulin in Chinese hamster ovary cells causes an increase in endogenous α-tubulin synthesis
    • Gonzalez-Garay, M.L., and F. Cabral. 1995. Overexpression of an epitopetagged β-tubulin in Chinese hamster ovary cells causes an increase in endogenous α-tubulin synthesis. Cell Motil. Cytoskeleton. 31:259-272.
    • (1995) Cell Motil. Cytoskeleton. , vol.31 , pp. 259-272
    • Gonzalez-Garay, M.L.1    Cabral, F.2
  • 13
    • 0021101284 scopus 로고
    • Expression of recombinant plasmids in mammalian cells is enhanced by sodium butyrate
    • Gorman, C.M., and B.H. Howard. 1983. Expression of recombinant plasmids in mammalian cells is enhanced by sodium butyrate. Nucleic Acids Res. 11: 7631-7648.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 7631-7648
    • Gorman, C.M.1    Howard, B.H.2
  • 14
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • Hershey, J.W.B. 1991. Translational control in mammalian cells. Annu. Rev. Biochem. 60:717-755.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 717-755
    • Hershey, J.W.B.1
  • 15
    • 0027360552 scopus 로고
    • Mechanism of mitotic block and inhibition of cell proliferation by taxol at low concentrations
    • Jordan, M.A., R.J. Toso, D. Thrower, and L. Wilson. 1993. Mechanism of mitotic block and inhibition of cell proliferation by taxol at low concentrations. Proc. Natl. Acad. Sci. USA. 90:9552-9556.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9552-9556
    • Jordan, M.A.1    Toso, R.J.2    Thrower, D.3    Wilson, L.4
  • 16
    • 0025063865 scopus 로고
    • Regulation of tubulin levels and microtubule assembly in Saccharomyces cerevisiae: Consequences of altered tubulin gene copy number
    • Katz, W., B. Weinstein, and F. Solomon. 1990. Regulation of tubulin levels and microtubule assembly in Saccharomyces cerevisiae: consequences of altered tubulin gene copy number. Mol. Cell. Biol. 10:5286-5292.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5286-5292
    • Katz, W.1    Weinstein, B.2    Solomon, F.3
  • 17
    • 0020422029 scopus 로고
    • The testis-specific β-tubulin subunit in Drosophila melanogaster has multiple functions in spermatogenesis
    • Kemphues, K.J., T.C. Kaufman, R.A. Raff, and E.C. Raff. 1982. The testis-specific β-tubulin subunit in Drosophila melanogaster has multiple functions in spermatogenesis. Cell. 31:655-670.
    • (1982) Cell , vol.31 , pp. 655-670
    • Kemphues, K.J.1    Kaufman, T.C.2    Raff, R.A.3    Raff, E.C.4
  • 18
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The control of cellular iron metabolism
    • Klausner, R.D., T.A. Rouault, and J.B. Harford. 1993. Regulating the fate of mRNA: the control of cellular iron metabolism. Cell. 72:19-28.
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 19
    • 0026937591 scopus 로고
    • Diversity of mechanisms in the regulation of translation in prokaryotes and lower eukaryotes
    • Lindahl, L., and A. Hinnebusch. 1992. Diversity of mechanisms in the regulation of translation in prokaryotes and lower eukaryotes. Curr. Opin. Genet. Dev. 2:720-726.
    • (1992) Curr. Opin. Genet. Dev. , vol.2 , pp. 720-726
    • Lindahl, L.1    Hinnebusch, A.2
  • 20
    • 0025108284 scopus 로고
    • Increasing tubC beta-tubulin synthesis by placing it under the control of a benA beta-tubulin upstream sequence causes a reduction in benA beta-tubulin level but has no effect on microtubule function
    • May, G.S., R.B. Waring, and N.R. Morris. 1990. Increasing tubC beta-tubulin synthesis by placing it under the control of a benA beta-tubulin upstream sequence causes a reduction in benA beta-tubulin level but has no effect on microtubule function. Cell Motil. Cytoskeleton. 16:214-220.
    • (1990) Cell Motil. Cytoskeleton. , vol.16 , pp. 214-220
    • May, G.S.1    Waring, R.B.2    Morris, N.R.3
  • 21
    • 0025872827 scopus 로고
    • Resistance to antimitotic drugs in Chinese hamster ovary cells correlates with changes in the level of polymerized tubulin
    • Minotti, A.M., S.B. Barlow, and F. Cabral. 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
  • 23
    • 0021155247 scopus 로고
    • Regulation of the synthesis of ribosomes and ribosomal components
    • Nomura, M., R. Gourse, and G. Baughman. 1984. Regulation of the synthesis of ribosomes and ribosomal components. Annu. Rev. Biochem. 53:75-117.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 75-117
    • Nomura, M.1    Gourse, R.2    Baughman, G.3
  • 24
    • 0024548940 scopus 로고
    • Expression and function of β-tubulin isotypes in Chinese hamster ovary cells
    • Sawada, T., and F. Cabral. 1989. Expression and function of β-tubulin isotypes in Chinese hamster ovary cells. J. Biol. Chem. 264:3013-3020.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3013-3020
    • Sawada, T.1    Cabral, F.2
  • 25
    • 0025291483 scopus 로고
    • In vivo discrimination among β-tubulin isotypes: Selective degradation of a type IV β-tubulin isotype following overexpression in cultured animal cells
    • Sisodia, S.S., D.A. Gay, and D.W. Cleveland. 1990. In vivo discrimination among β-tubulin isotypes: selective degradation of a type IV β-tubulin isotype following overexpression in cultured animal cells. New Biologist. 2:66-76.
    • (1990) New Biologist , vol.2 , pp. 66-76
    • Sisodia, S.S.1    Gay, D.A.2    Cleveland, D.W.3
  • 26
    • 0017659987 scopus 로고
    • Turnover of tubulin and the N site GTP in Chinese hamster ovary cells
    • Spiegelman, B.M., S.M. Penningroth, and M.W. Kirschner. 1977. Turnover of tubulin and the N site GTP in Chinese hamster ovary cells. Cell. 12:587-600.
    • (1977) Cell , vol.12 , pp. 587-600
    • Spiegelman, B.M.1    Penningroth, S.M.2    Kirschner, M.W.3
  • 27
    • 0028567464 scopus 로고
    • Regulation of translation by specific protein/mRNA interactions
    • Standart, N., and R.J. Jackson. 1994. Regulation of translation by specific protein/mRNA interactions. Biochimie (Paris). 76:867-879.
    • (1994) Biochimie (Paris) , vol.76 , pp. 867-879
    • Standart, N.1    Jackson, R.J.2
  • 28
    • 0024151129 scopus 로고
    • Structure and utilization of tubulin isotypes
    • Sullivan, K.F. 1988. Structure and utilization of tubulin isotypes. Annu. Rev. Cell Biol. 4:687-716.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 687-716
    • Sullivan, K.F.1
  • 29
    • 0026599699 scopus 로고
    • Physical evidence for cotranslational regulation of β-tubulin mRNA degradation
    • Theodorakis, N.G., and D.W. Cleveland. 1992. Physical evidence for cotranslational regulation of β-tubulin mRNA degradation. Mol. Cell. Biol. 12:791-799.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 791-799
    • Theodorakis, N.G.1    Cleveland, D.W.2
  • 30
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 31
    • 0022614233 scopus 로고
    • Transfer and amplification of a mutant β-tubulin gene results in colcemid dependence: Use of the transformant to demonstrate regulation of β-tubulin subunit levels by protein degradation
    • Whitfield, C., I. Abraham, D. Ascherman, and M.M. Gottesman. 1986. Transfer and amplification of a mutant β-tubulin gene results in colcemid dependence: use of the transformant to demonstrate regulation of β-tubulin subunit levels by protein degradation. Mol. Cell. Biol. 6:1422-1429.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 1422-1429
    • Whitfield, C.1    Abraham, I.2    Ascherman, D.3    Gottesman, M.M.4
  • 32
    • 0023941956 scopus 로고
    • Expression of a human α-tubulin: Properties of the isolated subunit
    • Yaffe, M.B., B.S. Levison, J. Szasz, and H. Sternlicht. 1988. Expression of a human α-tubulin: properties of the isolated subunit. Biochemistry. 27:1869-1880.
    • (1988) Biochemistry , vol.27 , pp. 1869-1880
    • Yaffe, M.B.1    Levison, B.S.2    Szasz, J.3    Sternlicht, H.4


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