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Volumn 17, Issue 4, 1997, Pages 2107-2115

Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; HEAT SHOCK PROTEIN; PHOSPHOPEPTIDE; SERINE; TRANSCRIPTION FACTOR;

EID: 0030988941     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.4.2107     Document Type: Article
Times cited : (251)

References (48)
  • 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. 1991. 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
    • 0029257329 scopus 로고
    • Inactivation of p42 MAP kinase by protein phosphatase 2a and a protein tyrosine phosphatase, but not CL100, in various cell lines
    • Alessi, D. R., N. Gomez, G. Moorhead, T. Lewis, S. M. Keyse, and P. Cohen. 1995. Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines. Curr. Biol. 5:283-295.
    • (1995) Curr. Biol. , vol.5 , pp. 283-295
    • Alessi, D.R.1    Gomez, N.2    Moorhead, G.3    Lewis, T.4    Keyse, S.M.5    Cohen, P.6
  • 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
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Boyle, W. J., P. van der Geer, and T. Hunter. 1991. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201:110-149.
    • (1991) Methods Enzymol. , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3
  • 6
    • 0029619815 scopus 로고
    • Activation of mitogen-activated protein kinase by heat shock treatment in Drosophila
    • Chen, F., M. Torres, and R. F. Duncan. 1995. Activation of mitogen-activated protein kinase by heat shock treatment in Drosophila. Biochem. J. 312: 341-349.
    • (1995) Biochem. J. , vol.312 , pp. 341-349
    • Chen, F.1    Torres, M.2    Duncan, R.F.3
  • 7
    • 0029846433 scopus 로고    scopus 로고
    • Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor 1
    • Chu, B., F. Soncin, B. D. Price, M. A. Stevenson, and S. K. Calderwood. 1996. Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor 1. J. Biol. Chem. 271:30847-30857.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30847-30857
    • Chu, B.1    Soncin, F.2    Price, B.D.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 8
    • 0025606431 scopus 로고
    • Molecular cloning and expression of a hexameric Drosophila heat shock factor subject to negative regulation
    • Clos, J., J. T. Westwood, P. B. Becker, S. Wilson, K. Lambert, and C. Wu. 1990. Molecular cloning and expression of a hexameric Drosophila heat shock factor subject to negative regulation. Cell 63:1085-1097.
    • (1990) Cell , vol.63 , pp. 1085-1097
    • Clos, J.1    Westwood, J.T.2    Becker, P.B.3    Wilson, S.4    Lambert, K.5    Wu, C.6
  • 9
    • 0029086379 scopus 로고
    • Stress causes induction of MAP kinase-specific phosphatase and rapid repression of MAP kinase activity in Drosophila
    • Cornelius, G., and M. Engel. 1995. Stress causes induction of MAP kinase-specific phosphatase and rapid repression of MAP kinase activity in Drosophila. Cell. Signalling 7:611-615.
    • (1995) Cell. Signalling , vol.7 , pp. 611-615
    • Cornelius, G.1    Engel, M.2
  • 10
    • 0030043401 scopus 로고    scopus 로고
    • Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation
    • Cotto, J. J., M. P. Kline, and R. I. Morimoto. 1996. Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation. J. Biol. Chem. 271:3355-3358.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3355-3358
    • Cotto, J.J.1    Kline, M.P.2    Morimoto, R.I.3
  • 11
    • 0027159874 scopus 로고
    • MAP kinase activation during heat shock in quiescent and exponentially growing mammalian cells
    • Dubois, M. F., and O. Bensaude. 1993. MAP kinase activation during heat shock in quiescent and exponentially growing mammalian cells. FEBS Lett. 324:191-195.
    • (1993) FEBS Lett. , vol.324 , pp. 191-195
    • Dubois, M.F.1    Bensaude, O.2
  • 13
    • 0029039963 scopus 로고
    • A heat shock-responsive domain of human HSF1 that regulates transcription activation domain function
    • Green, M., T. J. Schuetz, E. K. Sullivan, and R. E. Kingston. 1995. A heat shock-responsive domain of human HSF1 that regulates transcription activation domain function. Mol. Cell. Biol. 15:3354-3362.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3354-3362
    • Green, M.1    Schuetz, T.J.2    Sullivan, E.K.3    Kingston, R.E.4
  • 14
    • 0020577769 scopus 로고
    • Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: Skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed
    • Gunning, P., P. Ponte, H. Okayama, J. Engel, H. Blau, and L. Kedes. 1983. Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed. Mol. Cell. Biol. 3: 787-795.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 787-795
    • Gunning, P.1    Ponte, P.2    Okayama, H.3    Engel, J.4    Blau, H.5    Kedes, L.6
  • 15
    • 0028321786 scopus 로고
    • A short element required for turning off heat shock transcription factor: Evidence that phosphorylation enhances deactivation
    • Hoj, A., and B. K. Jakobsen. 1994. A short element required for turning off heat shock transcription factor: evidence that phosphorylation enhances deactivation. EMBO J. 13:2617-2624.
    • (1994) EMBO J. , vol.13 , pp. 2617-2624
    • Hoj, A.1    Jakobsen, B.K.2
  • 16
    • 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
  • 17
    • 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
  • 18
    • 0027113344 scopus 로고
    • Effect of sodium salicylate on the human heat shock response
    • Jurivich, D. A., L. Sistonen, R. A. Kroes, and R. I. Morimoto. 1992. Effect of sodium salicylate on the human heat shock response. Science 255:1243-1245.
    • (1992) Science , vol.255 , pp. 1243-1245
    • Jurivich, D.A.1    Sistonen, L.2    Kroes, R.A.3    Morimoto, R.I.4
  • 20
    • 0028846894 scopus 로고    scopus 로고
    • Salicylate triggers heat shock factor differently than heat
    • Jurivich, D. A., C. Pachetti, L. Qiu, and J. F. Welk. 1996. Salicylate triggers heat shock factor differently than heat. J. Biol. Chem. 270:24489-24495.
    • (1996) J. Biol. Chem. , vol.270 , pp. 24489-24495
    • Jurivich, D.A.1    Pachetti, C.2    Qiu, L.3    Welk, J.F.4
  • 21
    • 11944273348 scopus 로고
    • The protein kinase C-activated MAP kinase pathway of Saccharomyces cerevisiae mediates a novel aspect of the heat shock response
    • Kamada, Y., U. S. Jung, J. Piotrowski, and D. E. Levin. 1995. The protein kinase C-activated MAP kinase pathway of Saccharomyces cerevisiae mediates a novel aspect of the heat shock response. Genes Dev. 9:1559-1571.
    • (1995) Genes Dev. , vol.9 , pp. 1559-1571
    • Kamada, Y.1    Jung, U.S.2    Piotrowski, J.3    Levin, D.E.4
  • 22
    • 0028322193 scopus 로고
    • Signal transduction from the cell surface to the nucleus through the phosphorylation of transcription factors
    • Karin, M. 1994. Signal transduction from the cell surface to the nucleus through the phosphorylation of transcription factors. Curr. Opin. Cell. Biol. 6:415-424.
    • (1994) Curr. Opin. Cell. Biol. , vol.6 , pp. 415-424
    • Karin, M.1
  • 23
    • 0029804194 scopus 로고    scopus 로고
    • Repression of human heat shock factor 1 activity at control temperature by phosphorylation
    • Knauf, U., E. M. Newton, J. Kyriakis, and R. E. Kingston. 1996. Repression of human heat shock factor 1 activity at control temperature by phosphorylation. Genes Dev. 10:2782-2793.
    • (1996) Genes Dev. , vol.10 , pp. 2782-2793
    • Knauf, U.1    Newton, E.M.2    Kyriakis, J.3    Kingston, R.E.4
  • 24
    • 0027195230 scopus 로고
    • Mouse heat shock transcription factors 1 and 2 prefer a trimeric binding site but interact differently with the HSP70 heat shock element
    • Kroeger, P. E., K. D. Sarge, and R. I. Morimoto. 1993. Mouse heat shock transcription factors 1 and 2 prefer a trimeric binding site but interact differently with the HSP70 heat shock element. Mol. Cell. Biol. 13:3370-3383.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3370-3383
    • Kroeger, P.E.1    Sarge, K.D.2    Morimoto, R.I.3
  • 25
    • 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 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0023735270 scopus 로고
    • Activation in vitro of sequence-specific DNa binding by a human regulatory factor
    • Larson, J. S., T. J. Schuetz, and R. E. Kingston. 1988. Activation in vitro of sequence-specific DNA binding by a human regulatory factor. Nature 335: 372-375.
    • (1988) Nature , vol.335 , pp. 372-375
    • Larson, J.S.1    Schuetz, T.J.2    Kingston, R.E.3
  • 27
    • 0029161913 scopus 로고
    • Pharmacological modulation of heat shock factor 1 by anti-inflammatory drugs results in protection against stress-induced cellular damage
    • Lee, B. S., J. Chen, C. Angelidis, D. A. Jurivich, and R. I. Morimoto. 1995. Pharmacological modulation of heat shock factor 1 by anti-inflammatory drugs results in protection against stress-induced cellular damage. Proc. Natl. Acad. Sci. USA 92:7207-7211.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7207-7211
    • Lee, B.S.1    Chen, J.2    Angelidis, C.3    Jurivich, D.A.4    Morimoto, R.I.5
  • 28
    • 0029143041 scopus 로고
    • XCL100, an inducible nuclear MAP kinase phosphatase from Xenopus laevis: Its role in MAP kinase inactivation in differentiated cells and its expression during early development
    • Lewis, T., L. A. Groom, A. A. Sneddon, C. Smythe, and S. M. Keyse. 1995. XCL100, an inducible nuclear MAP kinase phosphatase from Xenopus laevis: its role in MAP kinase inactivation in differentiated cells and its expression during early development. J. Cell Sci. 108:2885-2896.
    • (1995) J. Cell Sci. , vol.108 , pp. 2885-2896
    • Lewis, T.1    Groom, L.A.2    Sneddon, A.A.3    Smythe, C.4    Keyse, S.M.5
  • 29
    • 0027220589 scopus 로고
    • Protein traffic on the heat shock promoter: Parking, stalling, and trucking along
    • Lis, J. T., and C. Wu. 1993. Protein traffic on the heat shock promoter: parking, stalling, and trucking along. Cell 74:1-4.
    • (1993) Cell , vol.74 , pp. 1-4
    • Lis, J.T.1    Wu, C.2
  • 30
    • 0028881937 scopus 로고
    • Mitogen-activated protein kinase acts as a negative regulator of the heat shock response in NIH3T3 cells
    • Mivechi, N. F., and A. J. Giaccia. 1995. Mitogen-activated protein kinase acts as a negative regulator of the heat shock response in NIH3T3 cells. Cancer Res. 55:5512-5519.
    • (1995) Cancer Res. , vol.55 , pp. 5512-5519
    • Mivechi, N.F.1    Giaccia, A.J.2
  • 31
    • 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
  • 33
    • 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
  • 34
    • 0027406535 scopus 로고
    • Characterization of a novel chicken heat shock transcription factor, heat shock factor 3, suggests a new regulatory pathway
    • Nakai, A., and R. I. Morimoto. 1993. Characterization of a novel chicken heat shock transcription factor, heat shock factor 3, suggests a new regulatory pathway. Mol. Cell. Biol. 13:1983-1997.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1983-1997
    • Nakai, A.1    Morimoto, R.I.2
  • 35
    • 0030049318 scopus 로고    scopus 로고
    • The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress
    • Newton, E. M., U. Knauf, M. Green, and R. E. Kingston. 1996. The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress. Mol. Cell. Biol. 16:839-846.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 839-846
    • Newton, E.M.1    Knauf, U.2    Green, M.3    Kingston, R.E.4
  • 36
    • 0027157980 scopus 로고
    • Rapid changes in Drosophila transcription after an instantaneous heat shock
    • O'Brien, T., and J. T. Lis. 1993. Rapid changes in Drosophila transcription after an instantaneous heat shock. Mol. Cell. Biol. 13:3456-3463.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3456-3463
    • O'Brien, T.1    Lis, J.T.2
  • 37
    • 0025864313 scopus 로고
    • Molecular cloning and expression of a human heat shock factor, HSF1
    • Rabindran, S. K., G. Giorgi, J. Clos, and C. Wu. 1991. Molecular cloning and expression of a human heat shock factor, HSF1. Proc. Natl. Acad. Sci. USA 88:6906-6910.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6906-6910
    • Rabindran, S.K.1    Giorgi, G.2    Clos, J.3    Wu, C.4
  • 38
    • 0027452754 scopus 로고
    • Regulation of heat shock factor trimer formation: Role of a conserved leucine zipper
    • Rabindran, S. K., R. I. Haroun, J. Clos, J. Wisniewski, and C. Wu. 1993. Regulation of heat shock factor trimer formation: role of a conserved leucine zipper. Science 259:230-234.
    • (1993) Science , vol.259 , pp. 230-234
    • Rabindran, S.K.1    Haroun, R.I.2    Clos, J.3    Wisniewski, J.4    Wu, C.5
  • 39
    • 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
  • 40
    • 0029025078 scopus 로고
    • The carboxyl-terminal transactivation domain of heat shock factor 1 is negatively regulated and stress responsive
    • Shi, Y., P. E. Kroeger, and R. I. Morimoto. 1995. The carboxyl-terminal transactivation domain of heat shock factor 1 is negatively regulated and stress responsive. Mol. Cell. Biol. 15:4309-4318.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4309-4318
    • Shi, Y.1    Kroeger, P.E.2    Morimoto, R.I.3
  • 41
    • 0024282785 scopus 로고
    • Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation
    • Sorger, P. K., and H. R. Pelham. 1988. Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation. Cell 54:855-864.
    • (1988) Cell , vol.54 , pp. 855-864
    • Sorger, P.K.1    Pelham, H.R.2
  • 42
    • 0024852809 scopus 로고
    • Trimerization of a yeast transcriptional activator via a coiled-coil motif
    • Sorger, P. K., and H. C. Nelson. 1989. Trimerization of a yeast transcriptional activator via a coiled-coil motif. Cell 59:807-813.
    • (1989) Cell , vol.59 , pp. 807-813
    • Sorger, P.K.1    Nelson, H.C.2
  • 43
    • 0027943988 scopus 로고
    • 2+/calmudulin-dependent protein kinases type II and type IV involves phosphorylation of a site that negatively regulates activity
    • 2+/calmudulin-dependent protein kinases type II and type IV involves phosphorylation of a site that negatively regulates activity. Genes Dev. 8:2527-2539.
    • (1994) Genes Dev. , vol.8 , pp. 2527-2539
    • Sun, P.1    Enslen, H.2    Myung, P.S.3    Maurer, R.A.4
  • 44
    • 0027159173 scopus 로고
    • Activation of Drosaphila heat shock factor: Conformational change associated with a monomer-to-trimer transition
    • Westwood, J. T., and C. Wu. 1993. Activation of Drosaphila heat shock factor: conformational change associated with a monomer-to-trimer transition. Mol. Cell. Biol. 13:3481-3486.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3481-3486
    • Westwood, J.T.1    Wu, C.2
  • 45
    • 0022002022 scopus 로고
    • Structure and expression of the human gene encoding major heat shock protein HSP70
    • Wu, B., C. Hunt, and R. I. Morimoto. 1985. Structure and expression of the human gene encoding major heat shock protein HSP70. Mol. Cell. Biol. 5: 330-341.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 330-341
    • Wu, B.1    Hunt, C.2    Morimoto, R.I.3
  • 46
    • 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
  • 47
    • 0028150986 scopus 로고
    • Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure
    • Zuo, J., R. Baler, G. Dahl, and R. Voellmy. 1994. Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure. Mol. Cell. Biol. 14:7557-7568.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7557-7568
    • Zuo, J.1    Baler, R.2    Dahl, G.3    Voellmy, R.4
  • 48
    • 0029055176 scopus 로고
    • Multiple layers of regulation of human heat shock factor 1
    • Zuo, J., D. Rungger, and R. Voellmy. 1995. Multiple layers of regulation of human heat shock factor 1. Mol. Cell. Biol. 15:4319-4330.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4319-4330
    • Zuo, J.1    Rungger, D.2    Voellmy, R.3


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