How to translate text using browser tools
1 November 2000 RSK2 represses HSF1 activation during heat shock
Xiaozhe Wang, Alexzander Asea, Yue Xie, Edith Kabingu, Mary Ann Stevenson, Stuart K. Calderwood
Author Affiliations +

Heat shock transcription factor 1(HSF1) activation is a multistep process. The conversion of a latent cytoplasmic form to a nuclear, DNA binding state appears to be activated by nonsteroidal anti-inflammatory drugs. In previous studies, we showed that HSF 1 is phosphorylated by the protein kinase RSK2 in vitro and that this effect is inhibited by nonsteroidal anti-inflammatory drugs at the concentration that leads to the activation of HSF1 in vivo (Stevenson et al 1999). In the present study, using cells from a patient with Coffin-Lowry syndrome (deficient in RSK2), we demonstrate that RSK2 slightly represses activation of HSF1 in vivo at 37°C. In Coffin-Lowry syndrome cells, HSF1-HSE DNA binding activity after treatment with sodium salicylate was slightly higher than that in untreated cells, indicating that although RSK2 is involved in HSF1 regulation, it is not the unique protein kinase that suppresses HSF1-HSE binding activity at 37°C. However, heat shock treatment resulted in significantly higher HSF1-HSE binding activity in Coffin-Lowry syndrome cells as compared with normal controls, suggesting that RSK2 represses HSF1-HSE binding activity during heat shock.

Xiaozhe Wang, Alexzander Asea, Yue Xie, Edith Kabingu, Mary Ann Stevenson, and Stuart K. Calderwood "RSK2 represses HSF1 activation during heat shock," Cell Stress & Chaperones 5(5), 432-437, (1 November 2000).<0432:RRHADH>2.0.CO;2
Received: 31 July 2000; Accepted: 1 August 2000; Published: 1 November 2000

This article is only available to subscribers.
It is not available for individual sale.

Get copyright permission
Back to Top