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Volumn 35, Issue 14, 2015, Pages 2530-2540

Uncoupling stress-inducible phosphorylation of heat shock factor 1 from its activation

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN A1A; HEAT SHOCK PROTEIN A1B; HEAT SHOCK PROTEIN B1; HEAT SHOCK TRANSCRIPTION FACTOR 1; MESSENGER RNA; UNCLASSIFIED DRUG; DNA; DNA BINDING PROTEIN; HSF1 PROTEIN, MOUSE; MUTANT PROTEIN; PROTEIN BINDING; TRANSCRIPTION FACTOR;

EID: 84932620032     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00816-14     Document Type: Article
Times cited : (76)

References (83)
  • 1
    • 79959463520 scopus 로고    scopus 로고
    • Regulation of HSF1 function in the heat stress response: implications in aging and disease
    • Anckar J, Sistonen L. 2011. Regulation of HSF1 function in the heat stress response: implications in aging and disease. Annu Rev Biochem 80:1089-1115. http://dx.doi.org/10.1146/annurev-biochem-060809-095203.
    • (2011) Annu Rev Biochem , vol.80 , pp. 1089-1115
    • Anckar, J.1    Sistonen, L.2
  • 2
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: life on the verge of death
    • Richter K, Haslbeck M, Buchner J. 2010. The heat shock response: life on the verge of death. Mol Cell 40:253-266. http://dx.doi.org/10.1016/j.molcel.2010.10.006.
    • (2010) Mol Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 3
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M. 2011. Molecular chaperones in protein folding and proteostasis. Nature 475:324-332. http://dx.doi.org/10.1038/nature10317.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 4
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: integrators of cell stress, development, and life span
    • Åkerfelt M, Morimoto RI, Sistonen L. 2010. Heat shock factors: integrators of cell stress, development, and life span. Nat Rev Mol Cell Biol 11: 545-555. http://dx.doi.org/10.1038/nrm2938.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 545-555
    • Åkerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 5
    • 0023694311 scopus 로고
    • Key features of heat shock regulatory elements
    • Amin J, Ananthan J, Voellmy R. 1988. Key features of heat shock regulatory elements. Mol Cell Biol 8:3761-3769.
    • (1988) Mol Cell Biol , vol.8 , pp. 3761-3769
    • Amin, J.1    Ananthan, J.2    Voellmy, R.3
  • 6
    • 0032936785 scopus 로고    scopus 로고
    • A new use for the 'wing' of the 'winged' helix-turn-helix motif in the HSF-DNA cocrystal
    • Littlefield O, Nelson HCM. 1999. A new use for the 'wing' of the 'winged' helix-turn-helix motif in the HSF-DNA cocrystal. Nat Struct Mol Biol 6:464-470. http://dx.doi.org/10.1038/8269.
    • (1999) Nat Struct Mol Biol , vol.6 , pp. 464-470
    • Littlefield, O.1    Nelson, H.C.M.2
  • 7
    • 1542373742 scopus 로고    scopus 로고
    • The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response
    • Trinklein ND, Murray JI, Hartman SJ, Botstein D, Myers RM. 2004. The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response. Mol Biol Cell 15:1254-1261. http://dx.doi.org/10.1091/mbc.E03-10-0738.
    • (2004) Mol Biol Cell , vol.15 , pp. 1254-1261
    • Trinklein, N.D.1    Murray, J.I.2    Hartman, S.J.3    Botstein, D.4    Myers, R.M.5
  • 9
    • 0032571397 scopus 로고    scopus 로고
    • Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis
    • McMillan DR, Xiao X, Shao L, Graves K, Benjamin IJ. 1998. Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis. J Biol Chem 273:7523-7528. http://dx.doi.org/10.1074/jbc.273.13.7523.
    • (1998) J Biol Chem , vol.273 , pp. 7523-7528
    • McMillan, D.R.1    Xiao, X.2    Shao, L.3    Graves, K.4    Benjamin, I.J.5
  • 10
    • 0033229880 scopus 로고    scopus 로고
    • HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice
    • Xiao X, Zuo X, Davis AA, McMillan DR, Curry BB, Richardson JA, Benjamin IJ. 1999. HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice. EMBO J 18:5943-5952. http://dx.doi.org/10.1093/emboj/18.21.5943.
    • (1999) EMBO J , vol.18 , pp. 5943-5952
    • Xiao, X.1    Zuo, X.2    Davis, A.A.3    McMillan, D.R.4    Curry, B.B.5    Richardson, J.A.6    Benjamin, I.J.7
  • 11
    • 0034641933 scopus 로고    scopus 로고
    • Embryonic development: maternal effect of Hsf1 on reproductive success
    • Christians E, Davis A, Thomas S, Benjamin I. 2000. Embryonic development: maternal effect of Hsf1 on reproductive success. Nature 407:693-694. http://dx.doi.org/10.1038/35037669.
    • (2000) Nature , vol.407 , pp. 693-694
    • Christians, E.1    Davis, A.2    Thomas, S.3    Benjamin, I.4
  • 12
    • 33751092252 scopus 로고    scopus 로고
    • Genome-wide analysis of human HSF1 signaling reveals a transcriptional program linked to cellular adaptation and survival
    • Page TJ, Sikder D, Yang L, Pluta L, Wolfinger RD, Kodadek T, Thomas RS. 2006. Genome-wide analysis of human HSF1 signaling reveals a transcriptional program linked to cellular adaptation and survival. Mol Biosystems 2:627-639. http://dx.doi.org/10.1039/b606129j.
    • (2006) Mol Biosystems , vol.2 , pp. 627-639
    • Page, T.J.1    Sikder, D.2    Yang, L.3    Pluta, L.4    Wolfinger, R.D.5    Kodadek, T.6    Thomas, R.S.7
  • 13
    • 0038701745 scopus 로고    scopus 로고
    • Regulation of aging and agerelated disease by DAF-16 and heat-shock factor
    • Hsu AL, Murphy CT, Kenyon C. 2003. Regulation of aging and agerelated disease by DAF-16 and heat-shock factor. Science 300:1142-1145. http://dx.doi.org/10.1126/science.1083701.
    • (2003) Science , vol.300 , pp. 1142-1145
    • Hsu, A.L.1    Murphy, C.T.2    Kenyon, C.3
  • 14
    • 0742323000 scopus 로고    scopus 로고
    • Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones
    • Morley JF, Morimoto RI. 2004. Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones. Mol Biol Cell 15:657-664. http://dx.doi.org/10.1091/mbc.E03-07-0532.
    • (2004) Mol Biol Cell , vol.15 , pp. 657-664
    • Morley, J.F.1    Morimoto, R.I.2
  • 17
    • 38949209515 scopus 로고    scopus 로고
    • Differential display of DNA-binding proteins reveals heat-shock factor 1 as a circadian transcription factor
    • Reinke H, Saini C, Fleury-Olela F, Dibner C, Benjamin IJ, Schibler U. 2008. Differential display of DNA-binding proteins reveals heat-shock factor 1 as a circadian transcription factor. Genes Dev 22:331-345. http://dx.doi.org/10.1101/gad.453808.
    • (2008) Genes Dev , vol.22 , pp. 331-345
    • Reinke, H.1    Saini, C.2    Fleury-Olela, F.3    Dibner, C.4    Benjamin, I.J.5    Schibler, U.6
  • 18
    • 34548658230 scopus 로고    scopus 로고
    • Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis
    • Dai C, Whitesell L, Rogers AB, Lindquist S. 2007. Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis. Cell 130:1005-1018. http://dx.doi.org/10.1016/j.cell.2007.07.020.
    • (2007) Cell , vol.130 , pp. 1005-1018
    • Dai, C.1    Whitesell, L.2    Rogers, A.B.3    Lindquist, S.4
  • 21
    • 0028500990 scopus 로고
    • Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor
    • Vuister GW, Kim S, Orosz A, Marquardt J, Wu C, Bax A. 1994. Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor. Nat Struct Biol 1:605-614. http://dx.doi.org/10.1038/nsb0994-605.
    • (1994) Nat Struct Biol , vol.1 , pp. 605-614
    • Vuister, G.W.1    Kim, S.2    Orosz, A.3    Marquardt, J.4    Wu, C.5    Bax, A.6
  • 22
    • 0030049318 scopus 로고    scopus 로고
    • The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress
    • Newton EM, Knauf U, Green M, Kingston RE. 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
  • 23
    • 0024852809 scopus 로고
    • Trimerization of a yeast transcriptional activator via a coiled-coil motif
    • Sorger PK, Nelson HCM. 1989. Trimerization of a yeast transcriptional activator via a coiled-coil motif. Cell 59:807-813. http://dx.doi.org/10.1016/0092-8674(89)90604-1.
    • (1989) Cell , vol.59 , pp. 807-813
    • Sorger, P.K.1    Nelson, H.C.M.2
  • 24
    • 0026621935 scopus 로고
    • Trimerization of the heat shock transcription factor by a triple-stranded α-helical coiled coil
    • Peteranderl R, Nelson HCM. 1992. Trimerization of the heat shock transcription factor by a triple-stranded α-helical coiled coil. Biochemistry 31:12272-12276. http://dx.doi.org/10.1021/bi00163a042.
    • (1992) Biochemistry , vol.31 , pp. 12272-12276
    • Peteranderl, R.1    Nelson, H.C.M.2
  • 25
    • 0027452754 scopus 로고
    • Regulation of heat shock factor trimer formation: role of a conserved leucine zipper
    • Rabindran SK, Haroun RI, Clos J, Wisniewski J, Wu C. 1993. Regulation of heat shock factor trimer formation: role of a conserved leucine zipper. Science 259:230-234. http://dx.doi.org/10.1126/science.8421783.
    • (1993) Science , vol.259 , pp. 230-234
    • Rabindran, S.K.1    Haroun, R.I.2    Clos, J.3    Wisniewski, J.4    Wu, C.5
  • 26
    • 0029055176 scopus 로고
    • Multiple layers of regulation of human heat shock transcription factor 1
    • Zuo J, Rungger D, Voellmy R. 1995. Multiple layers of regulation of human heat shock transcription 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
  • 27
    • 0029039963 scopus 로고
    • A heat shockresponsive domain of human HSF1 that regulates transcription activation domain function
    • Green M, Schuetz TJ, Sullivan EK, Kingston RE. 1995. A heat shockresponsive 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
  • 28
    • 70450209178 scopus 로고    scopus 로고
    • Mutational analysis of human heat-shock transcription factor 1 reveals a regulatory role for oligomerization in DNA-binding specificity
    • Takemori Y, Enoki Y, Yamamoto N, Fukai Y, Adachi K, Sakurai H. 2009. Mutational analysis of human heat-shock transcription factor 1 reveals a regulatory role for oligomerization in DNA-binding specificity. Biochem J 424:253-261. http://dx.doi.org/10.1042/BJ20090922.
    • (2009) Biochem J , vol.424 , pp. 253-261
    • Takemori, Y.1    Enoki, Y.2    Yamamoto, N.3    Fukai, Y.4    Adachi, K.5    Sakurai, H.6
  • 30
    • 18244384703 scopus 로고    scopus 로고
    • Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress
    • Guettouche T, Boellmann F, Lane WS, Voellmy R. 2005. Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress. BMC Biochem 6:4. http://dx.doi.org/10.1186/1471-2091-6-4.
    • (2005) BMC Biochem , vol.6 , pp. 4
    • Guettouche, T.1    Boellmann, F.2    Lane, W.S.3    Voellmy, R.4
  • 31
    • 60749101582 scopus 로고    scopus 로고
    • Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1
    • Westerheide SD, Anckar J, Stevens SM, Jr, Sistonen L, Morimoto RI. 2009. Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science 323:1063-1066. http://dx.doi.org/10.1126/science.1165946.
    • (2009) Science , vol.323 , pp. 1063-1066
    • Westerheide, S.D.1    Anckar, J.2    Stevens, S.M.3    Sistonen, L.4    Morimoto, R.I.5
  • 32
    • 84896843332 scopus 로고    scopus 로고
    • Interplay of acetyltransferase EP300 and the proteasome system in regulating heat shock transcription factor 1
    • Raychaudhuri S, Loew C, Körner R, Pinkert S, Theis M, Hayer-Hartl M, Buchholz F, Hartl FU. 2014. Interplay of acetyltransferase EP300 and the proteasome system in regulating heat shock transcription factor 1. Cell 156:975-985. http://dx.doi.org/10.1016/j.cell.2014.01.055.
    • (2014) Cell , vol.156 , pp. 975-985
    • Raychaudhuri, S.1    Loew, C.2    Körner, R.3    Pinkert, S.4    Theis, M.5    Hayer-Hartl, M.6    Buchholz, F.7    Hartl, F.U.8
  • 33
    • 84860623294 scopus 로고    scopus 로고
    • Post-translational modification of human heat shock factors and their functions: a recent update by proteomic approach
    • Xu YM, Huang DY, Chiu JF, Lau AT. 2012. Post-translational modification of human heat shock factors and their functions: a recent update by proteomic approach. J Proteome Res 11:2625-2634. http://dx.doi.org/10.1021/pr201151a.
    • (2012) J Proteome Res , vol.11 , pp. 2625-2634
    • Xu, Y.M.1    Huang, D.Y.2    Chiu, J.F.3    Lau, A.T.4
  • 34
    • 0029804194 scopus 로고    scopus 로고
    • Repression of human heat shock factor 1 activity at control temperature by phosphorylation
    • Knauf U, Newton EM, Kyriakis J, Kingston RE. 1996. Repression of human heat shock factor 1 activity at control temperature by phosphorylation. Genes Dev 10:2782-2793. http://dx.doi.org/10.1101/gad.10.21.2782.
    • (1996) Genes Dev , vol.10 , pp. 2782-2793
    • Knauf, U.1    Newton, E.M.2    Kyriakis, J.3    Kingston, R.E.4
  • 35
    • 0030988941 scopus 로고    scopus 로고
    • Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation
    • Kline MP, Morimoto RI. 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
  • 36
    • 0032541032 scopus 로고    scopus 로고
    • Transcriptional activity of heat shock factor 1 at 37°C is repressed through phosphorylation on two distinct serine residues by glycogen synthase kinase 3 and protein kinases Cα and Cζ
    • Chu B, Zhong R, Soncin F, Stevenson MA, Calderwood SK. 1998. Transcriptional activity of heat shock factor 1 at 37°C is repressed through phosphorylation on two distinct serine residues by glycogen synthase kinase 3 and protein kinases Cα and Cζ. J Biol Chem 273:18640-18646. http://dx.doi.org/10.1074/jbc.273.29.18640.
    • (1998) J Biol Chem , vol.273 , pp. 18640-18646
    • Chu, B.1    Zhong, R.2    Soncin, F.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 37
    • 0036901003 scopus 로고    scopus 로고
    • Multisite phosphorylation provides sophisticated regulation of transcription factors
    • Holmberg CI, Tran SE, Eriksson JE, Sistonen L. 2002. Multisite phosphorylation provides sophisticated regulation of transcription factors. Trends Biochem Sci 27:619-627. http://dx.doi.org/10.1016/S0968-0004(02)02207-7.
    • (2002) Trends Biochem Sci , vol.27 , pp. 619-627
    • Holmberg, C.I.1    Tran, S.E.2    Eriksson, J.E.3    Sistonen, L.4
  • 38
    • 0031055277 scopus 로고    scopus 로고
    • Hyperphosphorylation of heat shock transcription factor 1 is correlated with transcriptional competence and slow dissociation of active factor trimers
    • Xia W, Voellmy R. 1997. Hyperphosphorylation of heat shock transcription factor 1 is correlated with transcriptional competence and slow dissociation of active factor trimers. J Biol Chem 272:4094-4102. http://dx.doi.org/10.1074/jbc.272.7.4094.
    • (1997) J Biol Chem , vol.272 , pp. 4094-4102
    • Xia, W.1    Voellmy, R.2
  • 39
    • 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 JJ, Kline M, Morimoto RI. 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
  • 41
    • 0036290246 scopus 로고    scopus 로고
    • Blocking HSF1 by dominant-negative mutant to sensitize tumor cells to hyperthermia
    • Wang J, Yao M, Gu J, Sun L, Shen Y, Liu X. 2002. Blocking HSF1 by dominant-negative mutant to sensitize tumor cells to hyperthermia. Biochem Biophys Res Commun 290:1454-1461. http://dx.doi.org/10.1006/bbrc.2002.6373.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 1454-1461
    • Wang, J.1    Yao, M.2    Gu, J.3    Sun, L.4    Shen, Y.5    Liu, X.6
  • 42
    • 1642569697 scopus 로고    scopus 로고
    • DAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activity
    • Boellmann F, Guettouche T, Guo Y, Fenna M, Mnayer L, Voellmy R. 2004. DAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activity. Proc Natl Acad Sci U S A 101:4100-4105. http://dx.doi.org/10.1073/pnas.0304768101.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 4100-4105
    • Boellmann, F.1    Guettouche, T.2    Guo, Y.3    Fenna, M.4    Mnayer, L.5    Voellmy, R.6
  • 43
    • 67650410543 scopus 로고    scopus 로고
    • Biological and chemical approaches to diseases of proteostasis deficiency
    • Powers ET, Morimoto RI, Dillin A, Kelly JW, Balch WE. 2009. Biological and chemical approaches to diseases of proteostasis deficiency. Annu Rev Biochem 78:959-991. http://dx.doi.org/10.1146/annurev.biochem.052308.114844.
    • (2009) Annu Rev Biochem , vol.78 , pp. 959-991
    • Powers, E.T.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4    Balch, W.E.5
  • 44
    • 84874832163 scopus 로고    scopus 로고
    • Protein homeostasis as a therapeutic target for diseases of protein conformation
    • Calamini B, Morimoto RI. 2012. Protein homeostasis as a therapeutic target for diseases of protein conformation. Curr Top Med Chem 12: 2623-2640. http://dx.doi.org/10.2174/1568026611212220014.
    • (2012) Curr Top Med Chem , vol.12 , pp. 2623-2640
    • Calamini, B.1    Morimoto, R.I.2
  • 45
    • 25844466597 scopus 로고    scopus 로고
    • Heat shock response modulators as therapeutic tools for diseases of protein conformation
    • Westerheide SD, Morimoto RI. 2005. Heat shock response modulators as therapeutic tools for diseases of protein conformation. J Biol Chem 280: 33097-33100. http://dx.doi.org/10.1074/jbc.R500010200.
    • (2005) J Biol Chem , vol.280 , pp. 33097-33100
    • Westerheide, S.D.1    Morimoto, R.I.2
  • 46
    • 75749136948 scopus 로고    scopus 로고
    • Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease
    • Neef DW, Turski ML, Thiele DJ. 2010. Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease. PLoS Biol 8:e1000291. http://dx.doi.org/10.1371/journal.pbio.1000291.
    • (2010) PLoS Biol , vol.8
    • Neef, D.W.1    Turski, M.L.2    Thiele, D.J.3
  • 48
    • 84867502093 scopus 로고    scopus 로고
    • Small molecule activators of the heat shock response: chemical properties, molecular targets, and therapeutic promise
    • West JD, Wang Y, Morano KA. 2012. Small molecule activators of the heat shock response: chemical properties, molecular targets, and therapeutic promise. Chem Res Toxicol 25:2036-2053. http://dx.doi.org/10.1021/tx300264x.
    • (2012) Chem Res Toxicol , vol.25 , pp. 2036-2053
    • West, J.D.1    Wang, Y.2    Morano, K.A.3
  • 49
    • 0023697252 scopus 로고
    • GAL4-VP16 is an unusually potent transcriptional activator
    • Sadowski I, Ma J, Triezenberg S, Ptashne M. 1988. GAL4-VP16 is an unusually potent transcriptional activator. Nature 335:563-564. http://dx.doi.org/10.1038/335563a0.
    • (1988) Nature , vol.335 , pp. 563-564
    • Sadowski, I.1    Ma, J.2    Triezenberg, S.3    Ptashne, M.4
  • 50
    • 0023815651 scopus 로고
    • Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells
    • Mosser DD, Theodorakis NG, Morimoto RI. 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
  • 51
    • 0033669588 scopus 로고    scopus 로고
    • Formation of nuclear HSF1 granules varies depending on stress stimuli
    • Holmberg CI, Illman SA, Kallio M, Mikhailov A, Sistonen L. 2000. Formation of nuclear HSF1 granules varies depending on stress stimuli. Cell Stress Chaperones 5:219-228. http://dx.doi.org/10.1379/1466-1268(2000)005<0219:FONHGV>2.0.CO;2.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 219-228
    • Holmberg, C.I.1    Illman, S.A.2    Kallio, M.3    Mikhailov, A.4    Sistonen, L.5
  • 53
    • 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 KD, Murphy SP, Morimoto RI. 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
  • 54
    • 0027202187 scopus 로고
    • Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase
    • Zhuo S, Clemens JC, Hakes DJ, Barford D, Dixon JE. 1993. Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase. J Biol Chem 268:17754-17761.
    • (1993) J Biol Chem , vol.268 , pp. 17754-17761
    • Zhuo, S.1    Clemens, J.C.2    Hakes, D.J.3    Barford, D.4    Dixon, J.E.5
  • 55
    • 0346455771 scopus 로고    scopus 로고
    • The MDM2-p53 interaction
    • Moll UM, Petrenko O. 2003. The MDM2-p53 interaction. Mol Cancer Res 1:1001-1008.
    • (2003) Mol Cancer Res , vol.1 , pp. 1001-1008
    • Moll, U.M.1    Petrenko, O.2
  • 56
    • 0034818446 scopus 로고    scopus 로고
    • Post-translational modifications and activation of p53 by genotoxic stresses
    • Appella E, Anderson CW. 2001. Post-translational modifications and activation of p53 by genotoxic stresses. Eur J Biochem 268:2764-2772. http://dx.doi.org/10.1046/j.1432-1327.2001.02225.x.
    • (2001) Eur J Biochem , vol.268 , pp. 2764-2772
    • Appella, E.1    Anderson, C.W.2
  • 57
    • 0037075898 scopus 로고    scopus 로고
    • Activation of the p53 tumor suppressor protein
    • Vousden KH. 2002. Activation of the p53 tumor suppressor protein. Biochim Biophys Acta 1602:47-59. http://dx.doi.org/10.1016/S0304-419X(02)00035-5.
    • (2002) Biochim Biophys Acta , vol.1602 , pp. 47-59
    • Vousden, K.H.1
  • 58
    • 15044342095 scopus 로고    scopus 로고
    • Phosphorylation-dependent degradation of p300 by doxorubicin-activated p38 mitogen-activated protein kinase in cardiac cells
    • Poizat C, Puri PL, Bai Y, Kedes L. 2005. Phosphorylation-dependent degradation of p300 by doxorubicin-activated p38 mitogen-activated protein kinase in cardiac cells. Mol Cell Biol 25:2673-2687. http://dx.doi.org/10.1128/MCB.25.7.2673-2687.2005.
    • (2005) Mol Cell Biol , vol.25 , pp. 2673-2687
    • Poizat, C.1    Puri, P.L.2    Bai, Y.3    Kedes, L.4
  • 59
    • 0015216932 scopus 로고
    • The mechanism by which cycloheximide and related glutarimide antibiotics inhibit peptide synthesis on reticulocyte ribosomes
    • Obrig TG, Culp WJ, McKeehan WL, Hardesty B. 1971. The mechanism by which cycloheximide and related glutarimide antibiotics inhibit peptide synthesis on reticulocyte ribosomes. J Biol Chem 246:174-181.
    • (1971) J Biol Chem , vol.246 , pp. 174-181
    • Obrig, T.G.1    Culp, W.J.2    McKeehan, W.L.3    Hardesty, B.4
  • 60
    • 0031841818 scopus 로고    scopus 로고
    • Heat shock response and protein degradation: regulation of HSF2 by the ubiquitin-proteasome pathway
    • Mathew A, Mathur SK, Morimoto RI. 1998. Heat shock response and protein degradation: regulation of HSF2 by the ubiquitin-proteasome pathway. Mol Cell Biol 18:5091-5098.
    • (1998) Mol Cell Biol , vol.18 , pp. 5091-5098
    • Mathew, A.1    Mathur, S.K.2    Morimoto, R.I.3
  • 61
    • 79953699778 scopus 로고    scopus 로고
    • Anaphase-promoting complex/cyclosome participates in the acute response to protein-damaging stress
    • Ahlskog JK, Björk JK, Elsing AN, Aspelin C, Kallio M, Roos-Mattjus P, Sistonen L. 2010. Anaphase-promoting complex/cyclosome participates in the acute response to protein-damaging stress. Mol Cell Biol 30:5608-5620. http://dx.doi.org/10.1128/MCB.01506-09.
    • (2010) Mol Cell Biol , vol.30 , pp. 5608-5620
    • Ahlskog, J.K.1    Björk, J.K.2    Elsing, A.N.3    Aspelin, C.4    Kallio, M.5    Roos-Mattjus, P.6    Sistonen, L.7
  • 62
    • 0031467707 scopus 로고    scopus 로고
    • HSF1 granules: a novel stressinduced nuclear compartment of human cells
    • Cotto J, Fox S, Morimoto RI. 1997. HSF1 granules: a novel stressinduced nuclear compartment of human cells. J Cell Sci 110:2925-2934.
    • (1997) J Cell Sci , vol.110 , pp. 2925-2934
    • Cotto, J.1    Fox, S.2    Morimoto, R.I.3
  • 63
    • 0031452176 scopus 로고    scopus 로고
    • HSF1 transcription factor concentrates in nuclear foci during heat shock: relationship with transcription sites
    • Jolly C, Morimoto RI, Robert-Nicoud M, Vourc'h C. 1997. HSF1 transcription factor concentrates in nuclear foci during heat shock: relationship with transcription sites. J Cell Sci 110:2935-2941.
    • (1997) J Cell Sci , vol.110 , pp. 2935-2941
    • Jolly, C.1    Morimoto, R.I.2    Robert-Nicoud, M.3    Vourc'h, C.4
  • 64
    • 0041468990 scopus 로고    scopus 로고
    • Regulation of molecular chaperone gene transcription involves the serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic sequestration of heat shock factor 1
    • Wang X, Grammatikakis N, Siganou A, Calderwood SK. 2003. Regulation of molecular chaperone gene transcription involves the serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic sequestration of heat shock factor 1. Mol Cell Biol 23:6013-6026. http://dx.doi.org/10.1128/MCB.23.17.6013-6026.2003.
    • (2003) Mol Cell Biol , vol.23 , pp. 6013-6026
    • Wang, X.1    Grammatikakis, N.2    Siganou, A.3    Calderwood, S.K.4
  • 67
    • 0041827383 scopus 로고    scopus 로고
    • Formation of nuclear stress granules involves HSF2 and coincides with the nucleolar localization of Hsp70
    • Alastalo TP, Hellesuo M, Sandqvist A, Hietakangas V, Kallio M, Sistonen L. 2003. Formation of nuclear stress granules involves HSF2 and coincides with the nucleolar localization of Hsp70. J Cell Sci 116:3557-3570. http://dx.doi.org/10.1242/jcs.00671.
    • (2003) J Cell Sci , vol.116 , pp. 3557-3570
    • Alastalo, T.P.1    Hellesuo, M.2    Sandqvist, A.3    Hietakangas, V.4    Kallio, M.5    Sistonen, L.6
  • 68
    • 0032967906 scopus 로고    scopus 로고
    • Differential metal response and regulation of human heavy metal-inducible genes
    • Murata M, Gong P, Suzuki K, Koizumi S. 1999. Differential metal response and regulation of human heavy metal-inducible genes. J Cell Physiol 180:105-113. http://dx.doi.org/10.1002/(SICI)1097-4652(199907)180:1<105::AID-JCP12>3.0.CO;2-5.
    • (1999) J Cell Physiol , vol.180 , pp. 105-113
    • Murata, M.1    Gong, P.2    Suzuki, K.3    Koizumi, S.4
  • 69
    • 0742306280 scopus 로고    scopus 로고
    • Kinetics study of endogenous heat shock protein 70 expression
    • Wang S, Diller KR, Aggarwal SJ. 2003. Kinetics study of endogenous heat shock protein 70 expression. J Biomech Eng 125:794-797. http://dx.doi.org/10.1115/1.1632522.
    • (2003) J Biomech Eng , vol.125 , pp. 794-797
    • Wang, S.1    Diller, K.R.2    Aggarwal, S.J.3
  • 71
    • 84932607499 scopus 로고    scopus 로고
    • HSF1 regulation of beta-catenin in mammary cancer cells through control of HuR/elavL1 expression
    • Chou SD, Murshid A, Eguchi T, Gong J, Calderwood SK. 2015. HSF1 regulation of beta-catenin in mammary cancer cells through control of HuR/elavL1 expression. Oncogene 34:2178-2188. http://dx.doi.org/10.1038/onc.2014.177.
    • (2015) Oncogene , vol.34 , pp. 2178-2188
    • Chou, S.D.1    Murshid, A.2    Eguchi, T.3    Gong, J.4    Calderwood, S.K.5
  • 72
    • 84899754421 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib is a potent inducer of zinc-finger AN1-type domain 2a gene expression: role of HSF1/HSF2 heterocomplexes
    • Rossi A, Riccio A, Coccia M, Trotta E, La Frazia S, Santoro MG. 2014. The proteasome inhibitor bortezomib is a potent inducer of zinc-finger AN1-type domain 2a gene expression: role of HSF1/HSF2 heterocomplexes. J Biol Chem 289:12705-12715. http://dx.doi.org/10.1074/jbc.M113.513242.
    • (2014) J Biol Chem , vol.289 , pp. 12705-12715
    • Rossi, A.1    Riccio, A.2    Coccia, M.3    Trotta, E.4    La Frazia, S.5    Santoro, M.G.6
  • 75
    • 0026636883 scopus 로고
    • The regulation of transcription by phosphorylation
    • Hunter T, Karin M. 1992. The regulation of transcription by phosphorylation. Cell 70:375-387. http://dx.doi.org/10.1016/0092-8674(92)90162-6.
    • (1992) Cell , vol.70 , pp. 375-387
    • Hunter, T.1    Karin, M.2
  • 77
    • 0025032116 scopus 로고
    • Regulation of an enzyme by phosphorylation at the active site
    • Hurley JH, Dean AM, Sohl JL, Koshland DE, Jr, Stroud RM. 1990. Regulation of an enzyme by phosphorylation at the active site. Science 249:1012-1016. http://dx.doi.org/10.1126/science.2204109.
    • (1990) Science , vol.249 , pp. 1012-1016
    • Hurley, J.H.1    Dean, A.M.2    Sohl, J.L.3    Koshland, D.E.4    Stroud, R.M.5
  • 78
    • 0038623298 scopus 로고    scopus 로고
    • Localized recruitment of a chromatin-remodeling activity by an activator in vivo drives transcriptional elongation
    • Corey LL, Weirich CS, Benjamin IJ, Kingston RE. 2003. Localized recruitment of a chromatin-remodeling activity by an activator in vivo drives transcriptional elongation. Genes Dev 17:1392-1401. http://dx.doi.org/10.1101/gad.1071803.
    • (2003) Genes Dev , vol.17 , pp. 1392-1401
    • Corey, L.L.1    Weirich, C.S.2    Benjamin, I.J.3    Kingston, R.E.4
  • 79
    • 0034881496 scopus 로고    scopus 로고
    • Mediator, not holoenzyme, is directly recruited to the heat shock promoter by HSF upon heat shock
    • Park JM, Werner J, Kim JM, Lis JT, Kim Y. 2001. Mediator, not holoenzyme, is directly recruited to the heat shock promoter by HSF upon heat shock. Mol Cell 8:9-19. http://dx.doi.org/10.1016/S1097-2765(01)00296-9.
    • (2001) Mol Cell , vol.8 , pp. 9-19
    • Park, J.M.1    Werner, J.2    Kim, J.M.3    Lis, J.T.4    Kim, Y.5
  • 80
    • 0033664085 scopus 로고    scopus 로고
    • Potential targets for HSF1 within the preinitiation complex
    • Yuan C, Gurley WB. 2000. Potential targets for HSF1 within the preinitiation complex. Cell Stress Chaperones 5:229-242. http://dx.doi.org/10.1379/1466-1268(2000)005<0229:PTFHWT>2.0.CO;2.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 229-242
    • Yuan, C.1    Gurley, W.B.2
  • 82
    • 84895077483 scopus 로고    scopus 로고
    • Regulation of transcription factor activity by interconnected posttranslational modifications
    • Filtz TM, Vogel WK, Leid M. 2014. Regulation of transcription factor activity by interconnected posttranslational modifications. Trends Pharmacol Sci 35:76-85. http://dx.doi.org/10.1016/j.tips.2013.11.005.
    • (2014) Trends Pharmacol Sci , vol.35 , pp. 76-85
    • Filtz, T.M.1    Vogel, W.K.2    Leid, M.3
  • 83
    • 45749100074 scopus 로고    scopus 로고
    • Glutamine induces heat shock protein expression via O-glycosylation and phosphorylation of HSF-1 and Sp1
    • Singleton KD, Wischmeyer PE. 2008. Glutamine induces heat shock protein expression via O-glycosylation and phosphorylation of HSF-1 and Sp1. J Parent Enteral Nutr 32:371-376. http://dx.doi.org/10.1177/0148607108320661.
    • (2008) J Parent Enteral Nutr , vol.32 , pp. 371-376
    • Singleton, K.D.1    Wischmeyer, P.E.2


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