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Details on Person In the absence of stress HSF1 is predominantly monomeric and...

Class:IdSummation:4793891
_displayNameIn the absence of stress HSF1 is predominantly monomeric and...
_timestamp2014-02-18 03:33:21
created[InstanceEdit:4793886] Shamovsky, V, 2013-10-28
literatureReference[LiteratureReference:4793890] Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1
[LiteratureReference:4793726] Deciphering human heat shock transcription factor 1 regulation via post-translational modification in yeast
[LiteratureReference:4793649] Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
[LiteratureReference:4793878] Repression of human heat shock factor 1 activity at control temperature by phosphorylation
[LiteratureReference:4793647] Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex
[LiteratureReference:4793657] Multiple layers of regulation of human heat shock transcription factor 1
[LiteratureReference:4793641] Regulation of heat shock factor trimer formation: role of a conserved leucine zipper
[LiteratureReference:4793691] Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1
[LiteratureReference:5324655] HDAC6 controls major cell response pathways to cytotoxic accumulation of protein aggregates
modified[InstanceEdit:5096531] Shamovsky, V, 2013-11-11
[InstanceEdit:5324699] Shamovsky, V, 2014-02-18
textIn the absence of stress HSF1 is predominantly monomeric and is thought to be repressed in its inactive monomeric state by the following mechanisms:
  • interaction with chaperone proteins such as HSP90 (Zou J et al.1998; Guo Y et al. 2001)
  • intramolecular coiled-coil interactions between a hydrophobic leucine zipper domain in the carboxyl-terminus of the protein and three amino-terminal leucine zippers, which are required for homotrimerization and transcriptional activation (Rabindran SK et al. 1993; Zuo J et al. 1995)
  • post-translation modifications that include protein acetylation, sumoylation and phosphorylation may also contribute to HSF1 repression (Knauf U et al. 1996; Hietakangas V et al. 2003; Batista-Nascimento L et al. 2011)
The accumulation of misfolded proteins upon proteotoxic stresses leads to the release of HSF1 from the HSP90-containing multichaperone complex and results in HSF1 self-association to form homotrimers (Baler R et al. 1993). There is also evidence showing that HDAC6 senses the accumulation of misfolded, ubiquitinated protein aggregates in cells and induces dissociation of a repressive HDAC6:HSF1:HSP90 complex and subsequent HSF1 activation (Boyault C et al. 2007).
(summation)[Reaction:3371586] Dissociation of cytosolic HSF1:HSP90 complex [Homo sapiens]
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