Sequential Phosphorylation by Mitogen-activated Protein Kinase and Glycogen Synthase Kinase 3 Represses Transcriptional Activation by Heat Shock Factor-1*

@article{Chu1996SequentialPB,
  title={Sequential Phosphorylation by Mitogen-activated Protein Kinase and Glycogen Synthase Kinase 3 Represses Transcriptional Activation by Heat Shock Factor-1*},
  author={B. Chu and F. Soncin and B. Price and M. Stevenson and S. Calderwood},
  journal={The Journal of Biological Chemistry},
  year={1996},
  volume={271},
  pages={30847 - 30857}
}
Mammalian heat shock genes are regulated at the transcriptional level by heat shock factor-1 (HSF-1), a sequence-specific transcription factor. We have examined the role of serine phosphorylation of HSF-1 in the regulation of heat shock gene transcription. Our experiments show that mitogen-activated protein kinases (MAPKs) of the ERK-1 family phosphorylate HSF-1 on serine residues and repress the transcriptional activation of the heat shock protein 70B (HSP70B) promoter by HSF-1 in vivo. These… Expand
Transcriptional Activity of Heat Shock Factor 1 at 37 oC Is Repressed through Phosphorylation on Two Distinct Serine Residues by Glycogen Synthase Kinase 3α and Protein Kinases Cα and Cζ*
Heat shock factor 1 (HSF1) is the key transcriptional regulator of the heat shock genes that protect cells from environmental stress. However, because heat shock gene expression is deleterious toExpand
Regulation of Molecular Chaperone Gene Transcription Involves the Serine Phosphorylation, 14-3-3ε Binding, and Cytoplasmic Sequestration of Heat Shock Factor 1
TLDR
It is demonstrated for the first time that human HSF1 binds to the essential cell signaling protein 14-3-3ε and the serine phosphorylation-dependent binding results in the transcriptional repression ofHSF1 and its sequestration in the cytoplasm. Expand
c-Jun NH2-terminal Kinase Targeting and Phosphorylation of Heat Shock Factor-1 Suppress Its Transcriptional Activity*
TLDR
It is shown that c-Jun NH2-terminal kinase (JNK) phosphorylates HSF-1 and suppresses its transcriptional activity by rapidly clearing HSf-1 from the sites of transcription. Expand
Analysis of the phosphorylation of human heat shock transcription factor‐1 by MAP kinase family members
TLDR
The results show that HSF‐1 can be phosphorylated in a ras‐dependent manner by other members of the MAP kinase family such as JNK and p38 protein kinases and possibly others, and that ERK1 phosphorylation is dependent on a region of HSf‐1 extending from amino acids 280 to 308. Expand
Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2.
TLDR
It is demonstrated that HSF-1 is phosphorylated by CK2 on both serine and threonine residues and a phosphorylation site atThreonine 142 is characterized, which may be an essential step in the thermal activation of latent HSF1 by stresses. Expand
Association and Regulation of Heat Shock Transcription Factor 4b with both Extracellular Signal-Regulated Kinase Mitogen-Activated Protein Kinase and Dual-Specificity Tyrosine Phosphatase DUSP26
TLDR
It is shown that Hsf4b is a direct target of the mitogen-activated protein (MAP) kinase extracellular signal-related kinase (ERK) and that phosphorylation of Hsf 4b by ERK leads to increased ability of HSF4b to bind DNA. Expand
Glycogen Synthase Kinase 3β Negatively Regulates Both DNA-binding and Transcriptional Activities of Heat Shock Factor 1*
TLDR
The role of GSK3β as a negative regulator of HSF1 transcription in cells during heat shock is confirmed and it is demonstrated for the first time that GSK 3β functions to repress DNA binding. Expand
De-repression of heat shock transcription factor-1 in interleukin-6- treated hepatocytes is mediated by downregulation of glycogen synthase kinase 3beta and MAPK/ERK-1.
TLDR
It is shown that IL-6 has no direct effect on HSP 70 expression at 37 degrees C but does augment HSP70 expression in response to heat. Expand
Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation
TLDR
It is demonstrated that constitutive phosphorylation of HSF1 at serine residues distal to the transcriptional activation domain functions to repress transactivation to regulate transcriptional activity at control temperatures. Expand
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Examination of the basis for uncoupling the heat shock transcriptional response reveals that acquisition of the trimeric DNA binding state of HSF1 is independent of and precedes inducibly phosphorylation and furthermore that inducible phosphorylated correlates with transcriptional activation. Expand
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