c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity.

@article{Dai2000cJunNK,
  title={c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity.},
  author={Rujuan Dai and Wojciech Frejtag and Bo He and Yue Zhang and Nahid F Mivechi},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 24},
  pages={18210-8}
}
The mammalian heat shock transcription factor HSF-1 regulates the expression of the heat shock proteins, molecular chaperones that are involved in cellular processes from higher order assembly to protein degradation. HSF-1 is a phosphorylated monomer under physiological growth conditions and is located mainly in the cytoplasm. Upon activation by a variety of environmental stresses, HSF-1 is translocated into the nucleus, forms trimers, acquires DNA binding activity, is hyperphosphorylated… CONTINUE READING

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