Homologous Region 3 fromBombyx moriNucleopolyhedrovirus Enhancing the Transcriptional Activity of Heat Shock Cognate 70-4 Promoter fromBombyx moriandBombyx mandarinain Vitroandin Vivo

2005 ◽  
Vol 69 (5) ◽  
pp. 1014-1017 ◽  
Author(s):  
Shunming TANG ◽  
Qiaoling ZHAO ◽  
Yongzhu YI ◽  
Zhifang ZHANG ◽  
Yiren LI
Keyword(s):  
Heat Shock ◽  
Transcriptional Activity ◽  
Homologous Region ◽  
Heat Shock Cognate 70

scholarly journals Heat shock cognate 70 protein secretion as a new growth arrest signal for cancer cells

Oncogene ◽  
2009 ◽  
Vol 29 (1) ◽  
pp. 117-127 ◽  
Author(s):  
P Nirdé ◽  
D Derocq ◽  
M Maynadier ◽  
M Chambon ◽  
I Basile ◽  
...  
Keyword(s):  
Heat Shock ◽  
Cancer Cells ◽  
Protein Secretion ◽  
Growth Arrest ◽  
Heat Shock Cognate 70

Changes in the transcriptional activity of barley plastome genes under heat shock

2008 ◽  
Vol 55 (3) ◽  
pp. 293-300 ◽  
Author(s):  
Ya. O. Zubo ◽  
E. A. Lysenko ◽  
A. Yu. Aleinikova ◽  
V. V. Kusnetsov ◽  
N. L. Pshibytko
Keyword(s):  
Heat Shock ◽  
Transcriptional Activity

scholarly journals Glycogen Synthase Kinase 3β and Extracellular Signal-Regulated Kinase Inactivate Heat Shock Transcription Factor 1 by Facilitating the Disappearance of Transcriptionally Active Granules after Heat Shock

1998 ◽  
Vol 18 (11) ◽  
pp. 6624-6633 ◽  
Author(s):  
Bin He ◽  
Yong-Hong Meng ◽  
Nahid F. Mivechi
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Transcriptional Activity ◽  
Glycogen Synthase ◽  
Heat Shock Transcription Factor ◽  
Glycogen Synthase Kinase 3Β ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Gsk 3Β ◽  
Transcription Factor 1

ABSTRACT Heat shock transcription factor 1 (HSF-1) activates the transcription of heat shock genes in eukaryotes. Under normal physiological growth conditions, HSF-1 is a monomer. Its transcriptional activity is repressed by constitutive phosphorylation. Upon activation, HSF-1 forms trimers, acquires DNA binding activity, increases transcriptional activity, and appears as punctate granules in the nucleus. In this study, using bromouridine incorporation and confocal laser microscopy, we demonstrated that newly synthesized pre-mRNAs colocalize to the HSF-1 punctate granules after heat shock, suggesting that these granules are sites of transcription. We further present evidence that glycogen synthase kinase 3β (GSK-3β) and extracellular signal-regulated kinase mitogen-activated protein kinase (ERK MAPK) participate in the down regulation of HSF-1 transcriptional activity. Transient increases in the expression of GSK-3β facilitate the disappearance of HSF-1 punctate granules and reduce hsp-70 transcription after heat shock. We have also shown that ERK is the priming kinase for GSK-3β. Taken together, these results indicate that GSK-3β and ERK MAPK facilitate the inactivation of activated HSF-1 after heat shock by dispersing HSF-1 from the sites of transcription.

scholarly journals DAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activity

2004 ◽  
Vol 101 (12) ◽  
pp. 4100-4105 ◽  
Author(s):  
F. Boellmann ◽  
T. Guettouche ◽  
Y. Guo ◽  
M. Fenna ◽  
L. Mnayer ◽  
...  
Keyword(s):  
Heat Shock ◽  
Transcriptional Activity ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Stress Activation

scholarly journals AKT1 mediates multiple phosphorylation events that functionally promote HSF1 activation

2020 ◽  
Author(s):  
Wen-Cheng Lu ◽  
Ramsey Omari ◽  
Haimanti Ray ◽  
Richard L. Carpenter
Keyword(s):  
Heat Shock ◽  
Functional Role ◽  
Transcriptional Activity ◽  
Heat Shock Factor 1 ◽  
Heat Stress Response ◽  
Subsequent Investigation ◽  
Important Regulator ◽  
Shock Proteins ◽  
Hsf1 Gene

AbstractThe heat stress response activates the transcription factor heat shock factor 1 (HSF1), which subsequently upregulates heat shock proteins to maintain the integrity of the proteome. HSF1 activity requires nuclear localization, trimerization, DNA binding, phosphorylation, and gene transactivation. Phosphorylation at S326 is an important regulator of HSF1 transcriptional activity. Phosphorylation at S326 is mediated by AKT1, mTOR, p38, and MEK1. mTOR, p38, and MEK1 all phosphorylated S326 but AKT1 was the more potent activator. Mass spectrometry showed that AKT1 phosphorylated HSF1 at T142, S230, and T527 in addition to S326 whereas the other kinases did not. Subsequent investigation revealed that phosphorylation at T142 is necessary for HSF1 trimerization and that S230, S326, and T527 are required for HSF1 gene transactivation and recruitment of TFIIB and CDK9. This study suggests that HSF1 activity is regulated by phosphorylation at specific residues that promote different stages of HSF1 activation. Furthermore, this is the first study to identify the functional role of these phosphorylation events.

scholarly journals C-Terminus of Heat Shock Cognate 70 Interacting Protein Increases Following Stroke and Impairs Survival Against Acute Oxidative Stress

2011 ◽  
Vol 14 (10) ◽  
pp. 1787-1801 ◽  
Author(s):  
Jeannette N. Stankowski ◽  
Stephanie L.H. Zeiger ◽  
Evan L. Cohen ◽  
Donald B. DeFranco ◽  
Jiyang Cai ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Interacting Protein ◽  
C Terminus ◽  
Heat Shock Cognate 70

Heat shock-induced alterations in phosphorylation of the largest subunit of RNA polymerase II as revealed by monoclonal antibodies CC-3 and MPM-2

1999 ◽  
Vol 77 (4) ◽  
pp. 367-374 ◽  
Author(s):  
Sébastien B Lavoie ◽  
Alexandra L Albert ◽  
Alain Thibodeau ◽  
Michel Vincent
Keyword(s):  
Heat Shock ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcriptional Activity ◽  
Phosphorylation Sites ◽  
Stress Genes ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Heat Shocks ◽  
Carboxy Terminal

The phosphorylation of the carboxy-terminal domain of the largest subunit of RNA polymerase II plays an important role in the regulation of transcriptional activity and is also implicated in pre-mRNA processing. Different stresses, such as a heat shock, induce a marked alteration in the phosphorylation of this domain. The expression of stress genes by RNA polymerase II, to the detriment of other genes, could be attributable to such modifications of the phosphorylation sites. Using two phosphodependent antibodies recognizing distinct hyperphosphorylated forms of RNA polymerase II largest subunit, we studied the phosphorylation state of the subunit in different species after heat shocks of varying intensities. One of these antibodies, CC-3, preferentially recognizes the carboxy-terminal domain of the largest subunit under normal conditions, but its reactivity is diminished during stress. In contrast, the other antibody used, MPM-2, demonstrated a strong reactivity after a heat shock in most species studied. Therefore, CC-3 and MPM-2 antibodies discriminate between phosphoisomers that may be functionally different. Our results further indicate that the pattern of phosphorylation of RNA polymerase II in most species varies in response to environmental stress.Key words: RNA polymerase II, heat shock, phosphorylation, CC-3, MPM-2.

Sign in / Sign up

Export Citation Format

Share Document