Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation. Evidence for a multistep pathway of regulation
- PMID: 8631933
- DOI: 10.1074/jbc.271.7.3355
Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation. Evidence for a multistep pathway of regulation
Abstract
Exposure of mammalian cells in culture to the anti-inflammatory drugs sodium salicylate or indomethacin results in activation of heat shock factor 1 (HSF1) DNA binding activity. We have previously shown that the drug-induced HSF1 becomes associated with the heat shock elements of the hsp70 promoter, yet transcription of the hsp70 gene is not induced (Jurivich, D. A., Sistonen, L., Kroes, R. A., and Morimoto, R. I. (1992) Science 255, 1243-1245). In this study, we have examined the basis for uncoupling the heat shock transcriptional response. Comparison of heat shock and drug-induced forms of HSF1 has revealed that the transcriptionally inert drug-induced HSF1 is constitutively but not inducibly serine-phosphorylated, whereas heat shock-induced HSF1 is both constitutively and inducibly serine-phosphorylated. The transcriptionally inert intermediate represented by drug-induced HSF1 can be converted to the transcriptionally active state by a subsequent exposure to heat shock. The only detectable change in HSF1 is the acquisition of inducible serine phosphorylation. These data reveal that acquisition of the trimeric DNA binding state of HSF1 is independent of and precedes inducible phosphorylation and furthermore that inducible phosphorylation correlates with transcriptional activation.
Similar articles
-
Salicylate triggers heat shock factor differently than heat.J Biol Chem. 1995 Oct 13;270(41):24489-95. doi: 10.1074/jbc.270.41.24489. J Biol Chem. 1995. PMID: 7592665
-
mTOR is essential for the proteotoxic stress response, HSF1 activation and heat shock protein synthesis.PLoS One. 2012;7(6):e39679. doi: 10.1371/journal.pone.0039679. Epub 2012 Jun 29. PLoS One. 2012. PMID: 22768106 Free PMC article.
-
JNK phosphorylates the HSF1 transcriptional activation domain: role of JNK in the regulation of the heat shock response.J Cell Biochem. 2001;82(2):326-38. doi: 10.1002/jcb.1163. J Cell Biochem. 2001. PMID: 11527157
-
Implication of reactive oxygen species, ERK1/2, and p38MAPK in sodium salicylate-induced heat shock protein 72 expression in C6 glioma cells.Int J Mol Med. 2005 Nov;16(5):841-9. Int J Mol Med. 2005. PMID: 16211253
-
Regulation of the mammalian heat shock factor 1.FEBS J. 2017 Jun;284(11):1606-1627. doi: 10.1111/febs.13999. Epub 2017 Feb 1. FEBS J. 2017. PMID: 28052564 Review.
Cited by
-
Phosphorylation of the yeast heat shock transcription factor is implicated in gene-specific activation dependent on the architecture of the heat shock element.Mol Cell Biol. 2004 May;24(9):3648-59. doi: 10.1128/MCB.24.9.3648-3659.2004. Mol Cell Biol. 2004. PMID: 15082761 Free PMC article.
-
Modulation of Akt and ERK1/2 pathways by resveratrol in chronic myelogenous leukemia (CML) cells results in the downregulation of Hsp70.PLoS One. 2010 Jan 14;5(1):e8719. doi: 10.1371/journal.pone.0008719. PLoS One. 2010. PMID: 20090934 Free PMC article.
-
Poly(ADP-Ribose) Polymerase 1 Promotes the Human Heat Shock Response by Facilitating Heat Shock Transcription Factor 1 Binding to DNA.Mol Cell Biol. 2018 Jun 14;38(13):e00051-18. doi: 10.1128/MCB.00051-18. Print 2018 Jul 1. Mol Cell Biol. 2018. PMID: 29661921 Free PMC article.
-
Increased temperature and protein oxidation lead to HSP72 mRNA and protein accumulation in the in vivo exercised rat heart.Exp Physiol. 2009 Jan;94(1):71-80. doi: 10.1113/expphysiol.2008.044685. Epub 2008 Oct 17. Exp Physiol. 2009. PMID: 18931043 Free PMC article.
-
Activation of heat-shock transcription factor 1 by hypertonic shock in 3T3 cells.Biochem J. 1996 Oct 15;319 ( Pt 2)(Pt 2):601-6. doi: 10.1042/bj3190601. Biochem J. 1996. PMID: 8912700 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
