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p(HGNC:HSF1)

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Entity

Name
HSF1
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 8

The Biology of Proteostasis in Aging and Disease v1.0.0

A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways v1.0.0

Promoting the clearance of neurotoxic proteins in neurodegenerative disorders of ageing v1.0.0

Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0

Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity v1.0.0

Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0

Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection v1.0.0

Molecular chaperones and proteostasis regulation during redox imbalance v1.0.0

In-Edges 16

complex(a(MESH:"Molecular Chaperones"), p(HGNC:HSF1)) hasComponent p(HGNC:HSF1) View Subject | View Object

Appears in Networks:

a(PUBCHEM:377503130) increases act(p(HGNC:HSF1)) View Subject | View Object

High-throughput screens in yeast and HeLa cells identified HSF1A and F1, respectively, as two small molecules that activate HSF1 independently of HSP90 inhibition (136, 137). PubMed:25784053

Appears in Networks:
Annotations
Cell Ontology (CL)
motor neuron

bp(GO:"response to misfolded protein") increases act(p(HGNC:HSF1)) View Subject | View Object

Upon increased levels of nonnative proteins, HSF1 is released from its repressive complex, acquires DNA-binding activity through homotrimerization, and rapidly translocates to the nucleus to induce expression of genes encoding molecular chaperones (7, 35). PubMed:25784053

Appears in Networks:

complex(a(MESH:"Molecular Chaperones"), p(HGNC:HSF1)) decreases act(p(HGNC:HSF1)) View Subject | View Object

Once stress has been relieved, HSF1 activity is repressed through acetylation and binding to molecular chaperones (34, 36, 37). PubMed:25784053

Appears in Networks:

act(p(HGNC:HSF1)) increases tloc(p(HGNC:HSF1), fromLoc(MESH:Cytosol), toLoc(MESH:"Cell Nucleus")) View Subject | View Object

Upon increased levels of nonnative proteins, HSF1 is released from its repressive complex, acquires DNA-binding activity through homotrimerization, and rapidly translocates to the nucleus to induce expression of genes encoding molecular chaperones (7, 35). PubMed:25784053

Appears in Networks:

p(FPLX:"CCT_complex") decreases act(p(HGNC:HSF1)) View Subject | View Object

HSF1A suppresses toxicity in cell and tissue culture models of HD and SCA-3/MJD and appears to activate HSF1 by impairing the activity of TRiC, a recently discovered negative regulator of HSF1. PubMed:25784053

Appears in Networks:
Annotations
Cell Ontology (CL)
motor neuron

act(p(FPLX:HSP90)) decreases act(p(HGNC:HSF1)) View Subject | View Object

One strategy is to directly activate HSF1, thereby increasing the expression of multiple molecular chaperones simultaneously. This approach has been traditionally achieved by inhibition of HSP90 with compounds that bind the N-terminal ATP-binding pocket, such as radicicol, geldanamycin, or 17-AAG (64, 132–134). PubMed:25784053

Appears in Networks:
Annotations
Cell Ontology (CL)
motor neuron

p(HGNC:HSF1, pmod(Ac)) decreases act(p(HGNC:HSF1)) View Subject | View Object

Once stress has been relieved, HSF1 activity is repressed through acetylation and binding to molecular chaperones (34, 36, 37). PubMed:25784053

Appears in Networks:

path(MESH:Neoplasms) association act(p(HGNC:HSF1)) View Subject | View Object

Constitutive activation of HSF1 is detrimental to cells and increased expression, and activity of HSF1 has been linked to multiple forms of cancer, highlighting the need for appropriate and balanced activation of stress response pathways as and when required throughout life (122). PubMed:25784053

Appears in Networks:
Annotations
Cell Ontology (CL)
motor neuron

complex(p(HGNC:BAG3), p(HGNC:HSF1)) hasComponent p(HGNC:HSF1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:HSF1), p(HGNC:TP53), p(INTERPRO:"Heat shock protein 70 family")) hasComponent p(HGNC:HSF1) View Subject | View Object

Appears in Networks:

a(PUBCHEM:9568077) increases act(p(HGNC:HSF1), ma(tscript)) View Subject | View Object

One promising agent is the hydroxylamine deriva- tive arimoclomol, which increases the activity of HSP70 by augmenting transcriptional activity of HSF1 (REF.210) . PubMed:30116051

Appears in Networks:

a(CHEBI:geldanamycin) increases act(p(HGNC:HSF1)) View Subject | View Object

For exam- ple, small molecules (e.g., geldanamycin) that activate heat shock factor 1, the main transcrip- tional regulator of the cytosolic stress response, increase the effective concentration of cytosolic chaperones and suppress the aggregation of various disease proteins (8, 38, 228–230). PubMed:23746257

Appears in Networks:

bp(GO:"Hsp90 deacetylation") increases act(p(HGNC:HSF1)) View Subject | View Object

HDAC6 activity was also reported to regulate chaperone expression in response to heat shock by deacetylating Hsp90 leading to release and activation of the transcription factor HSF-1 [79]. PubMed:18930136

Appears in Networks:

bp(GO:"response to stress") increases p(HGNC:HSF1, loc(MESH:"Cell Nucleus")) View Subject | View Object

During elevated stress the chaperones within the repressive HSF1-containing multi-chaperone complexes bind the unfolded proteins and thus the liberated monomeric HSF1s undergo phosphorylation, trimerization and nuclear localization with increased transcriptional activity [109]. PubMed:24563850

Appears in Networks:

bp(GO:"response to stress") increases act(p(HGNC:HSF1), ma(tscript)) View Subject | View Object

During elevated stress the chaperones within the repressive HSF1-containing multi-chaperone complexes bind the unfolded proteins and thus the liberated monomeric HSF1s undergo phosphorylation, trimerization and nuclear localization with increased transcriptional activity [109]. PubMed:24563850

Appears in Networks:

Out-Edges 13

p(HGNC:HSF1) hasVariant p(HGNC:HSF1, pmod(Ac)) View Subject | View Object

Appears in Networks:

act(p(HGNC:HSF1)) increases tloc(p(HGNC:HSF1), fromLoc(MESH:Cytosol), toLoc(MESH:"Cell Nucleus")) View Subject | View Object

Upon increased levels of nonnative proteins, HSF1 is released from its repressive complex, acquires DNA-binding activity through homotrimerization, and rapidly translocates to the nucleus to induce expression of genes encoding molecular chaperones (7, 35). PubMed:25784053

Appears in Networks:

act(p(HGNC:HSF1), ma(tscript)) increases a(MESH:"Molecular Chaperones") View Subject | View Object

Upon increased levels of nonnative proteins, HSF1 is released from its repressive complex, acquires DNA-binding activity through homotrimerization, and rapidly translocates to the nucleus to induce expression of genes encoding molecular chaperones (7, 35). PubMed:25784053

Appears in Networks:

act(p(HGNC:HSF1)) association path(MESH:Neoplasms) View Subject | View Object

Constitutive activation of HSF1 is detrimental to cells and increased expression, and activity of HSF1 has been linked to multiple forms of cancer, highlighting the need for appropriate and balanced activation of stress response pathways as and when required throughout life (122). PubMed:25784053

Appears in Networks:
Annotations
Cell Ontology (CL)
motor neuron

act(p(HGNC:HSF1), ma(tscript)) increases act(p(FPLX:HSPA)) View Subject | View Object

One promising agent is the hydroxylamine deriva- tive arimoclomol, which increases the activity of HSP70 by augmenting transcriptional activity of HSF1 (REF.210) . PubMed:30116051

Appears in Networks:

p(HGNC:HSF1) increases a(MESH:"Heat-Shock Proteins") View Subject | View Object

The expression of Hsps is regulated by heat shock factor 1 (HSF1), which, under stress conditions, becomes associated with heat shock elements to elevate the transcription of Hsps and other proteins [51]. PubMed:21882945

Appears in Networks:

p(HGNC:HSF1) increases bp(HBP:Proteostasis) View Subject | View Object

However, the mechanisms that link HSF1 induction to improved proteostasis are not yet clear PubMed:21882945

Appears in Networks:

p(HGNC:HSF1) increases bp(HBP:Proteostasis) View Subject | View Object

Therapeutic approaches to overcome proteostasis deficiencies have largely focused on the activation of HSF1, the heat shock transcription factor responsible for simultaneous upregulation of the expression of multiple molecular chaperones during stress (Calamini et al., 2011; Pierce et al., 2013). PubMed:27491084

Appears in Networks:

p(HGNC:HSF1) regulates bp(GO:"cellular response to stress") View Subject | View Object

For exam- ple, small molecules (e.g., geldanamycin) that activate heat shock factor 1, the main transcrip- tional regulator of the cytosolic stress response, increase the effective concentration of cytosolic chaperones and suppress the aggregation of various disease proteins (8, 38, 228–230). PubMed:23746257

Appears in Networks:

p(HGNC:HSF1) increases a(MESH:"Molecular Chaperones") View Subject | View Object

For exam- ple, small molecules (e.g., geldanamycin) that activate heat shock factor 1, the main transcrip- tional regulator of the cytosolic stress response, increase the effective concentration of cytosolic chaperones and suppress the aggregation of various disease proteins (8, 38, 228–230). PubMed:23746257

Appears in Networks:

p(HGNC:HSF1) decreases a(MESH:"Protein Aggregates") View Subject | View Object

For exam- ple, small molecules (e.g., geldanamycin) that activate heat shock factor 1, the main transcrip- tional regulator of the cytosolic stress response, increase the effective concentration of cytosolic chaperones and suppress the aggregation of various disease proteins (8, 38, 228–230). PubMed:23746257

Appears in Networks:

p(HGNC:HSF1) hasVariant p(HGNC:HSF1, pmod(Ph)) View Subject | View Object

Appears in Networks:

p(HGNC:HSF1) increases a(MESH:"Heat-Shock Proteins") View Subject | View Object

HSF1 binds to a consensus heat shock element (HSE) within the promoter regions of HSP genes resulting in the activation of HSPs' gene expression and the control of cellular responses to oxidative and proteotoxic stress [108]. PubMed:24563850

Appears in Networks:

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.