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Volumn 88, Issue 3, 2005, Pages 1646-1658

Mathematical modeling of the eukaryotic heat-shock response: Dynamics of the hsp70 promoter

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DNA; HEAT SHOCK PROTEIN 70; HEAT SHOCK TRANSCRIPTION FACTOR 1; MESSENGER RNA; DNA BINDING PROTEIN; HEAT SHOCK TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR;

EID: 21244495733     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.055301     Document Type: Article
Times cited : (79)

References (53)
  • 1
    • 0025935407 scopus 로고
    • Attenuation of the heat-shock response in Hela-cells is mediated by the release of bound heat-shock transcription factor and is modulated by changes in growth and in heat-shock temperatures
    • Abravaya, K., B. Phillips, and R. I. Morimoto. 1991a. Attenuation of the heat-shock response in Hela-cells is mediated by the release of bound heat-shock transcription factor and is modulated by changes in growth and in heat-shock temperatures. Genes Dev. 5:2117-2127.
    • (1991) Genes Dev. , vol.5 , pp. 2117-2127
    • Abravaya, K.1    Phillips, B.2    Morimoto, R.I.3
  • 2
    • 0026033076 scopus 로고
    • Heat-shock-induced interactions of heat-shock transcription factor and the human hsp70 promoter examined by in vivo footprinting
    • Abravaya, K., B. Phillips, and R. I. Morimoto. 1991b. Heat-shock-induced interactions of heat-shock transcription factor and the human hsp70 promoter examined by in vivo footprinting. Mol. Cell. Biol. 11:586-592.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 586-592
    • Abravaya, K.1    Phillips, B.2    Morimoto, R.I.3
  • 3
    • 0034914737 scopus 로고    scopus 로고
    • A computational study of feedback effects on signal dynamics in a mitogen-activated protein kinase (MAPK) pathway model
    • Asthagiri, A. R., and D. A. Lauffenburger. 2001. A computational study of feedback effects on signal dynamics in a mitogen-activated protein kinase (MAPK) pathway model. Biotechnol. Prog. 17:227-239.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 227-239
    • Asthagiri, A.R.1    Lauffenburger, D.A.2
  • 4
    • 0027474909 scopus 로고
    • Activation of human heat-shock genes is accompanied by oligomerization, modification, and rapid translocation of heat-shock transcription factor HSF1
    • Baler, R., G. Dahl, and R. Voellmy. 1993. Activation of human heat-shock genes is accompanied by oligomerization, modification, and rapid translocation of heat-shock transcription factor HSF1. Mol. Cell. Biol. 13:2486-2496.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2486-2496
    • Baler, R.1    Dahl, G.2    Voellmy, R.3
  • 5
    • 0038701684 scopus 로고    scopus 로고
    • Huntingtin aggregation and toxicity in Huntington's disease
    • Bates, G. 2003. Huntingtin aggregation and toxicity in Huntington's disease. Lancet. 361:1642-1644.
    • (2003) Lancet , vol.361 , pp. 1642-1644
    • Bates, G.1
  • 6
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B., and A. L. Horwich. 1998. The Hsp70 and Hsp60 chaperone machines. Cell. 92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 7
    • 0030043401 scopus 로고    scopus 로고
    • Activation of heat-shock factor 1 DNA binding precedes stress-induced serine phosphorylation. Evidence for a multistep pathway of regulation
    • Cotto, J. J., M. Kline, and R. I. Morimoto. 1996. Activation of heat-shock factor 1 DNA binding precedes stress-induced serine phosphorylation. Evidence for a multistep pathway of regulation. J. Biol. Chem. 271:3355-3358.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3355-3358
    • Cotto, J.J.1    Kline, M.2    Morimoto, R.I.3
  • 8
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • Cyr, D. M., J. Hohfeld, and C. Patterson. 2002. Protein quality control: U-box-containing E3 ubiquitin ligases join the fold. Trends Biochem. Sci. 27:368-375.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 368-375
    • Cyr, D.M.1    Hohfeld, J.2    Patterson, C.3
  • 9
    • 0021228666 scopus 로고
    • Heat-shock-induced translational alterations in HeLa cells. Initiation factor modifications and the inhibition of translation
    • Duncan, R., and J. W. Hershey. 1984. Heat-shock-induced translational alterations in HeLa cells. Initiation factor modifications and the inhibition of translation. J. Biol. Chem. 259:11882-11889.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11882-11889
    • Duncan, R.1    Hershey, J.W.2
  • 10
    • 0033570071 scopus 로고    scopus 로고
    • Striking multiplicity of eIF4E-BP1 phosphorylated isoforms identified by 2D gel electrophoresis regulation by heat-shock
    • Duncan, R. F., and H. J. Song. 1999. Striking multiplicity of eIF4E-BP1 phosphorylated isoforms identified by 2D gel electrophoresis regulation by heat-shock. Eur. J. Biochem. 265:728-743.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 728-743
    • Duncan, R.F.1    Song, H.J.2
  • 12
    • 0030445778 scopus 로고    scopus 로고
    • Tripping the switch fantastic: How a protein kinase cascade can convert graded inputs into switch-like outputs
    • Ferrell, J. E., Jr. 1996. Tripping the switch fantastic: how a protein kinase cascade can convert graded inputs into switch-like outputs. Trends Biochem. Sci. 21:460-466.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 460-466
    • Ferrell Jr., J.E.1
  • 13
    • 0031203921 scopus 로고    scopus 로고
    • How responses get more switch-like as you move down a protein kinase cascade
    • Ferrell, J. E., Jr. 1997. How responses get more switch-like as you move down a protein kinase cascade. Trends Biochem. Sci. 22:288-289.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 288-289
    • Ferrell Jr., J.E.1
  • 14
    • 0035162698 scopus 로고    scopus 로고
    • Genomic expression responses to DNA-damaging agents and the regulatory role of the yeast ATR homolog Mec1p
    • Gasch, A. P., M. Huang, S. Metzner, D. Botstein, S. J. Elledge, and P. O. Brown. 2001. Genomic expression responses to DNA-damaging agents and the regulatory role of the yeast ATR homolog Mec1p. Mol. Biol. Cell. 12:2987-3003.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2987-3003
    • Gasch, A.P.1    Huang, M.2    Metzner, S.3    Botstein, D.4    Elledge, S.J.5    Brown, P.O.6
  • 15
    • 0001424903 scopus 로고
    • An amplified sensitivity arising from covalent modification in biological systems
    • Goldbeter, A., and D. E. Koshland, Jr. 1981. An amplified sensitivity arising from covalent modification in biological systems. Proc. Natl. Acad. Sci. USA. 78:6840-6844.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6840-6844
    • Goldbeter, A.1    Koshland Jr., D.E.2
  • 17
    • 0036901003 scopus 로고    scopus 로고
    • Multisite phosphorylation provides sophisticated regulation of transcription factors
    • Holmberg, C. I., S. E. Tran, J. E. Eriksson, and L. Sistonen. 2002. Multisite phosphorylation provides sophisticated regulation of transcription factors. Trends Biochem. Sci. 27:619-627.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 619-627
    • Holmberg, C.I.1    Tran, S.E.2    Eriksson, J.E.3    Sistonen, L.4
  • 19
    • 0029790351 scopus 로고    scopus 로고
    • Ultrasensitivity in the mitogen-activated protein kinase cascade
    • Huang, C. Y., and J. E. Ferrell, Jr. 1996. Ultrasensitivity in the mitogen-activated protein kinase cascade. Proc. Natl. Acad. Sci. USA. 93:10078-10083.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10078-10083
    • Huang, C.Y.1    Ferrell Jr., J.E.2
  • 20
    • 0026636883 scopus 로고
    • The regulation of transcription by phosphorylation
    • Hunter, T., and M. Karin. 1992. The regulation of transcription by phosphorylation. Cell. 70:375-387.
    • (1992) Cell , vol.70 , pp. 375-387
    • Hunter, T.1    Karin, M.2
  • 21
    • 0026559568 scopus 로고
    • Regulating transcription factor activity by phosphorylation
    • Jackson, S. P. 1992. Regulating transcription factor activity by phosphorylation. Trends Cell Biol. 2:104-108.
    • (1992) Trends Cell Biol. , vol.2 , pp. 104-108
    • Jackson, S.P.1
  • 22
    • 0023701108 scopus 로고
    • Constitutive binding of yeast heat-shock factor to DNA in vivo
    • Jakobsen, B. K., and H. R. Pelham. 1988. Constitutive binding of yeast heat-shock factor to DNA in vivo. Mol. Cell. Biol. 8:5040-5042.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5040-5042
    • Jakobsen, B.K.1    Pelham, H.R.2
  • 23
    • 0023094286 scopus 로고
    • Heat-inducible human factor that binds to a human hsp70 promoter
    • Kingston, R. E., T. J. Schuetz, and Z. Larin. 1987. Heat-inducible human factor that binds to a human hsp70 promoter. Mol. Cell. Biol. 7:1530-1534.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1530-1534
    • Kingston, R.E.1    Schuetz, T.J.2    Larin, Z.3
  • 24
    • 0030988941 scopus 로고    scopus 로고
    • Repression of the heat-shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation
    • Kline, M. P., and R. I. Morimoto. 1997. Repression of the heat-shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation. Mol. Cell. Biol. 17:2107-2115.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2107-2115
    • Kline, M.P.1    Morimoto, R.I.2
  • 26
    • 0026935588 scopus 로고
    • Heat-shock proteins and stress tolerance in microorganisms
    • Lindquist, S. 1992. Heat-shock proteins and stress tolerance in microorganisms. Curr. Opin. Genet. Dev. 2:748-755.
    • (1992) Curr. Opin. Genet. Dev. , vol.2 , pp. 748-755
    • Lindquist, S.1
  • 27
    • 0029664413 scopus 로고    scopus 로고
    • Oxidative stress induced heat-shock factor phosphorylation and HSF-dependent activation of yeast metallothionein gene transcription
    • Liu, X. D., and D. J. Thiele. 1996. Oxidative stress induced heat-shock factor phosphorylation and HSF-dependent activation of yeast metallothionein gene transcription. Genes Dev. 10:592-603.
    • (1996) Genes Dev. , vol.10 , pp. 592-603
    • Liu, X.D.1    Thiele, D.J.2
  • 29
    • 0043180477 scopus 로고    scopus 로고
    • Oscillatory expression of Hes1, p53, and NF-κB driven by transcriptional time delays
    • Monk, N. A. 2003. Oscillatory expression of Hes1, p53, and NF-κB driven by transcriptional time delays. Curr. Biol. 13:1409-1413.
    • (2003) Curr. Biol. , vol.13 , pp. 1409-1413
    • Monk, N.A.1
  • 30
    • 0027522356 scopus 로고
    • Cells in stress-transcriptional activation of heat-shock genes
    • Morimoto, R. I. 1993. Cells in stress-transcriptional activation of heat-shock genes. Science. 259:1409-1410.
    • (1993) Science , vol.259 , pp. 1409-1410
    • Morimoto, R.I.1
  • 31
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat-shock transcriptional response: Cross talk between a family of heat-shock factors, molecular chaperones, and negative regulators
    • Morimoto, R. I. 1998. Regulation of the heat-shock transcriptional response: cross talk between a family of heat-shock factors, molecular chaperones, and negative regulators. Genes Dev. 12:3788-3796.
    • (1998) Genes Dev. , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 32
    • 0026592050 scopus 로고
    • Transcriptional regulation of heat-shock genes. A paradigm for inducible genomic responses
    • Morimoto, R. I., K. D. Sarge, and K. Abravaya. 1992. Transcriptional regulation of heat-shock genes. A paradigm for inducible genomic responses. J. Biol. Chem. 267:21987-21990.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21987-21990
    • Morimoto, R.I.1    Sarge, K.D.2    Abravaya, K.3
  • 33
    • 0742323000 scopus 로고    scopus 로고
    • Regulation of longevity in Caenorhabditis elegans by heat-shock factor and molecular chaperones
    • Morley, J. F., and R. I. Morimoto. 2004. Regulation of longevity in Caenorhabditis elegans by heat-shock factor and molecular chaperones. Mol. Biol. Cell. 15:657-664.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 657-664
    • Morley, J.F.1    Morimoto, R.I.2
  • 34
    • 0023815651 scopus 로고
    • Coordinate changes in heat-shock element-binding activity and hsp70 gene transcription rates in human cells
    • Mosser, D. D., N. G. Theodorakis, and R. I. Morimoto. 1988. Coordinate changes in heat-shock element-binding activity and hsp70 gene transcription rates in human cells. Mol. Cell. Biol. 8:4736-4744.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4736-4744
    • Mosser, D.D.1    Theodorakis, N.G.2    Morimoto, R.I.3
  • 35
    • 0037099046 scopus 로고    scopus 로고
    • Chaperoning signaling pathways: Molecular chaperones as stress-sensing "heat-shock" proteins
    • Nollen, E. A., and R. I. Morimoto. 2002. Chaperoning signaling pathways: molecular chaperones as stress-sensing "heat-shock" proteins. J. Cell Sci. 115:2809-2816.
    • (2002) J. Cell Sci. , vol.115 , pp. 2809-2816
    • Nollen, E.A.1    Morimoto, R.I.2
  • 36
    • 0023169857 scopus 로고
    • On the dynamics of the irreversible Michaelis-Menten reaction mechanism
    • Palsson, B. O. 1987. On the dynamics of the irreversible Michaelis-Menten reaction mechanism. Chem. Eng. Sci. 42:447-458.
    • (1987) Chem. Eng. Sci. , vol.42 , pp. 447-458
    • Palsson, B.O.1
  • 37
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell, D. A., and S. Lindquist. 1993. The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Genet. 27:437-496.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 38
    • 0020184673 scopus 로고
    • A regulatory upstream promoter element in the Drosophila hsp70 heat-shock gene
    • Pelham, H. R. 1982. A regulatory upstream promoter element in the Drosophila hsp70 heat-shock gene. Cell. 30:517-528.
    • (1982) Cell , vol.30 , pp. 517-528
    • Pelham, H.R.1
  • 40
    • 17744372861 scopus 로고    scopus 로고
    • Roles of the heat-shock transcription factors in regulation of the heat-shock response and beyond
    • Pirkkala, L., P. Nykanen, and L. Sistonen. 2001. Roles of the heat-shock transcription factors in regulation of the heat-shock response and beyond. FASEB J. 15:1118-1131.
    • (2001) FASEB J. , vol.15 , pp. 1118-1131
    • Pirkkala, L.1    Nykanen, P.2    Sistonen, L.3
  • 41
    • 0006921595 scopus 로고
    • Near-equilibrium reaction and the regulation of pathways
    • Reich, J. G. 1974. Near-equilibrium reaction and the regulation of pathways. Symp. Biolog. Hungarica. 18:159-171.
    • (1974) Symp. Biolog. Hungarica , vol.18 , pp. 159-171
    • Reich, J.G.1
  • 42
    • 0027461364 scopus 로고
    • Activation of heat-shock gene transcription by heat-shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress
    • Sarge, K. D., S. P. Murphy, and R. I. Morimoto. 1993. Activation of heat-shock gene transcription by heat-shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress. Mol. Cell. Biol. 13:1392-1407.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1392-1407
    • Sarge, K.D.1    Murphy, S.P.2    Morimoto, R.I.3
  • 44
    • 0024731820 scopus 로고
    • The quasi-steady-state assumption - A case-study in perturbation
    • Segel, L. A., and M. Slemrod. 1989. The quasi-steady-state assumption-a case-study in perturbation. SIAM Rev. 31:446-477.
    • (1989) SIAM Rev. , vol.31 , pp. 446-477
    • Segel, L.A.1    Slemrod, M.2
  • 45
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressors
    • Shi, Y., D. D. Mosser, and R. I. Morimoto. 1998. Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 12:654-666.
    • (1998) Genes Dev. , vol.12 , pp. 654-666
    • Shi, Y.1    Mosser, D.D.2    Morimoto, R.I.3
  • 46
    • 0023643235 scopus 로고
    • Heat-shock factor is regulated differently in yeast and HeLa cells
    • Sorger, P. K., M. J. Lewis, and H. R. B. Pelham. 1987. Heat-shock factor is regulated differently in yeast and HeLa cells. Nature. 329:81-84.
    • (1987) Nature , vol.329 , pp. 81-84
    • Sorger, P.K.1    Lewis, M.J.2    Pelham, H.R.B.3
  • 48
    • 0023511826 scopus 로고
    • Posttranscriptional regulation of hsp70 expression in human cells-effects of heat-shock, inhibition of protein synthesis, and Adenovirus infection on translation and messenger-RNA stability
    • Theodorakis, N. G., and R. I. Morimoto. 1987. Posttranscriptional regulation of hsp70 expression in human cells-effects of heat-shock, inhibition of protein synthesis, and Adenovirus infection on translation and messenger-RNA stability. Mol. Cell. Biol. 7:4357-4368.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 4357-4368
    • Theodorakis, N.G.1    Morimoto, R.I.2
  • 49
    • 0000481011 scopus 로고
    • Sensitivity analysis of complex kinetic systems-tools and applications
    • Turanyi, T. 1990. Sensitivity analysis of complex kinetic systems-tools and applications. J. Math. Chem. 5:203-248.
    • (1990) J. Math. Chem. , vol.5 , pp. 203-248
    • Turanyi, T.1
  • 51
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Foldine, refolding, and degrading proteins
    • Wickner, S., M. R. Maurizi, and S. Gottesman. 1999. Posttranslational quality control: foldine, refolding, and degrading proteins. Science. 286:1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 52
    • 0029564954 scopus 로고
    • Heat-shock transcription factors: Structure and regulation
    • Wu, C. 1995. Heat-shock transcription factors: structure and regulation. Annu. Rev. Cell Dev. Biol. 11:441-469.
    • (1995) Annu. Rev. Cell Dev. Biol. , vol.11 , pp. 441-469
    • Wu, C.1
  • 53
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat-shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou, J., Y. Guo, T. Guettouche, D. F. Smith, and R. Voellmy. 1998. Repression of heat-shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell. 94:471-480.
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5


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