Abstract
In concert with the stress-induced activation of human heat shock factor 1 (HSF1), the factor becomes inducibly phosphorylated and accumulates into nuclear granules. To date, these processes are not fully understood. Here, we show that although stress caused by the proteasome inhibitors MG132 and clasto-lactacystine beta-lactone induces the expression of Hsp70, the formation of HSF1 granules is affected differently in comparison to heat shock. Furthermore, proteasome inhibition increases serine phosphorylation on HSF1, but to a lesser extent than heat stress. Our results suggest that, depending on the type of stress stimulus, the multiple events associated with HSF1 activation might be affected differently.
| Original language | English |
|---|---|
| Pages (from-to) | 219-28 |
| Number of pages | 10 |
| Journal | Cell Stress and Chaperones |
| Volume | 5 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Jul 2000 |
| MoE publication type | A1 Journal article-refereed |
Keywords
- Blotting, Western
- Cell Nucleus Structures/metabolism
- Cysteine Endopeptidases/drug effects
- Cysteine Proteinase Inhibitors/pharmacology
- DNA-Binding Proteins/metabolism
- HSP70 Heat-Shock Proteins/genetics
- HeLa Cells
- Heat Shock Transcription Factors
- Heat-Shock Proteins/metabolism
- Heat-Shock Response
- Humans
- K562 Cells
- Lactones/pharmacology
- Leupeptins/pharmacology
- Microscopy, Fluorescence
- Multienzyme Complexes/antagonists & inhibitors
- Phosphorylation/drug effects
- Promoter Regions, Genetic/genetics
- Proteasome Endopeptidase Complex
- Recombinant Proteins/immunology
- Transcription Factors