Formation of nuclear HSF1 granules varies depending on stress stimuli

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: Holmberg CI, Illman SA, Kallio M, Mikhailov A, Sistonen L
Publisher: CELL STRESS SOC INTERNATIONAL
Publication year: 2000
Journal: Cell Stress and Chaperones
Journal acronym: CELL STRESS CHAPERON
Volume number: 5
Issue number: 3
Start page: 219
End page: 228
Number of pages: 10
ISSN: 1355-8145


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.

Last updated on 2019-20-10 at 03:08