Analysis of the phosphorylation of human heat shock transcription factor-1 by MAP kinase family members

Jynho Kim, Arsenio Nueda, Yong Hong Meng, William S. Dynan, Nahid F. Mivechi

Research output: Contribution to journalArticlepeer-review

51 Scopus citations


The activation of heat shock transcription factor-1 (HSF-1) after treatment of mammalian cells with stresses such as heat shock, heavy metals, or ethanol induces the synthesis of heat shock proteins. HSF-1 is phosphorylated at normal growth temperature and is hyperphosphorylated upon stress. We recently presented evidence that HSF-1 can be phosphorylated by the mitogen activated protein kinase, ERK1, and that such phosphorylation appears to negatively regulate the activity of HSF-1. In this report, we have tested the ability of ERK1 to phosphorylate various HSF-1 deletion mutants. Our results show that ERK1 phosphorylation is dependent on a region of HSF-1 extending from amino acids 280 to 308. This region contains three serine residues that are potential ERK1 phosphorylation sites. The region falls within a previously defined regulatory domain of HSF-1. The possibility of protein kinases other than ERK1 phosphorylating HSF-1 was also examined using in-gel kinase assays. 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.

Original languageEnglish (US)
Pages (from-to)43-54
Number of pages12
JournalJournal of cellular biochemistry
Issue number1
StatePublished - Oct 1 1997


  • ERK1
  • HSF-1
  • Heat shock
  • MAP kinases
  • Phosphorylation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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