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Details on Person Acquisition of DNA binding activity by HSF1 is necessary but...
| Class:Id | Summation:5083657 |
|---|---|
| _displayName | Acquisition of DNA binding activity by HSF1 is necessary but... |
| _timestamp | 2016-03-17 14:29:49 |
| created | [InstanceEdit:5083642] Shamovsky, V, 2013-11-07 |
| literatureReference | [LiteratureReference:5083639] A heat shock-responsive domain of human HSF1 that regulates transcription activation domain function [LiteratureReference:5083649] The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress [LiteratureReference:5083670] Transcriptional activation domains stimulate initiation and elongation at different times and via different residues [LiteratureReference:4793657] Multiple layers of regulation of human heat shock transcription factor 1 [LiteratureReference:5082377] Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress [LiteratureReference:5082414] Phosphorylation of serine 230 promotes inducible transcriptional activity of heat shock factor 1 [LiteratureReference:4793824] Heat shock factor-1 protein in heat shock factor-1 gene-transfected human epidermoid A431 cells requires phosphorylation before inducing heat shock protein-70 production [LiteratureReference:5083663] Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation [LiteratureReference:5083675] Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation. Evidence for a multistep pathway of regulation [LiteratureReference:4793807] The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response |
| modified | [InstanceEdit:5096431] Shamovsky, V, 2013-11-09 [InstanceEdit:5577005] Matthews, Lisa, 2014-05-28 [InstanceEdit:8864981] Shamovsky, Veronica, 2016-03-17 |
| text | Acquisition of DNA binding activity by HSF1 is necessary but insufficient for transcriptional activation (Cotto JJ et al. 1996; Trinklein ND et al. 2004). In addition to having a sequence-specific DNA binding domain, HSF1 contains a C-terminal region which is involved in activating the transcription of the target genes (Green M et al. 1995). However, the transactivating ability of the transactivation domain itself is not stress sensitive. Rather, it's controled by a regulatory domain of HSF1 (amino acids 221-310), which represses the transactivating ability under normal physiological conditions (Green M et al. 1995; Zuo J et al. 1995; Newton EM et al. 1996). The HSF1 transactivation domain can be divided into two distinct regions, activation domain 1 (AD1) and activation domain 2 (AD2) (Brown SA et al. 1998). AD1 and AD2 each contain residues that are important for both transcriptional initiation and elongation. Mutations in acidic residues in both AD1 and AD2 preferentially affect the ability of HSF1 to stimulate transcriptional initiation, while mutations in phenylalanine residues preferentially affect stimulation of elongation (Brown SA et al. 1998). Activation of the DNA-bound but transcriptionally incompetent HSF1 is thought to occur upon stress induced HSF1 phosphorylation at several serine residues (Ding XZ et al. 1997; Holmberg CI et al. 2001; Guettouche T et al. 2005). In cells exposed to heat, acquisition of HSE DNA-binding activity was observed to precede phosphorylation of HSF1 (Cotto JJ et al. 1996; Kline MP & Morimoto RI 1997). While there is a sufficient evidence to suggest that phosphorylation of HSF1 is essential to modulate HSF1 transactiviting capacity, mechanisms behind stress stimuli and kinases/phosphatases involved have not been clearly established. |
| (summation) | [Pathway:3371571] HSF1-dependent transactivation [Homo sapiens] |
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