Analysis of the phosphorylation of human heat shock transcription factor-1 by MAP kinase family members
| Autor: | J, Kim, A, Nueda, Y H, Meng, W S, Dynan, N F, Mivechi |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Mitogen-Activated Protein Kinase 3
Recombinant Fusion Proteins JNK Mitogen-Activated Protein Kinases 3T3 Cells p38 Mitogen-Activated Protein Kinases DNA-Binding Proteins Mice Heat Shock Transcription Factors Calcium-Calmodulin-Dependent Protein Kinases Serine ras Proteins Animals Humans Mitogen-Activated Protein Kinases Phosphorylation Heat-Shock Proteins Heat-Shock Response Sequence Deletion Transcription Factors |
| Zdroj: | Journal of cellular biochemistry. 67(1) |
| ISSN: | 0730-2312 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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