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Details on Person The inactive HSF1 was reported to constitutively shuttle bet...

Class:IdSummation:5336204
_displayNameThe inactive HSF1 was reported to constitutively shuttle bet...
_timestamp2014-03-02 05:00:30
created[InstanceEdit:5336205] Shamovsky, V, 2014-03-02
literatureReference[LiteratureReference:4793704] Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress
[LiteratureReference:4793657] Multiple layers of regulation of human heat shock transcription factor 1
[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: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:4793850] Human heat shock factor 1 is predominantly a nuclear protein before and after heat stress
[LiteratureReference:4793714] Constitutive nuclear import and stress-regulated nucleocytoplasmic shuttling of mammalian heat-shock factor 1
textThe inactive HSF1 was reported to constitutively shuttle between the nucleus and the cytoplasm in mammalian cells (Vujanac M et al. 2005). There is no consensus on whether inactive HSF1 monomers localize in the nucleus or in the cytosol (Sarge KD et al. 1993; Zuo J et al. 1995; Mercier PA et al. 1999; Vujanac M et al. 2005). This event shows stress-induced activation of HSF1 in the nucleus.

In 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).
(summation)[Reaction:5082409] Dissociation of HSF1:HSP90 complex in the nucleus [Homo sapiens]
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