1. Catalog
  2. Nodes
  3. p(FPLX:HSPA)

p(FPLX:HSPA)

Equivalencies: 0 | Classes: 1 | Children: 0 | Explore

Entity

Name
HSPA
Namespace
FPLX
Namespace Version
20180917
Namespace URL
https://raw.githubusercontent.com/sorgerlab/famplex/e8ae9926ff95266032cb74f77973c84939bffbeb/export/famplex.belns

Appears in Networks 8

A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease. v1.0.0

The Ubiquitin Proteasome System in Neurodegenerative Diseases: Sometimes the Chicken, Sometimes the Egg v1.0.0

The Biology of Proteostasis in Aging and Disease v1.0.0

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

Clearance of Amyloid Beta and Tau in Alzheimer’s Disease:from Mechanisms to Therapy v1.0.1

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

Molecular chaperones and proteostasis regulation during redox imbalance v1.0.0

In-Edges 28

a(CHEBI:ATP) association act(p(FPLX:HSPA)) View Subject | View Object

The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566

Appears in Networks:

bp(MESH:Aging) decreases p(FPLX:HSPA) View Subject | View Object

Among the genes that are repressed in both aging and AD, the HSP70- HSP40 system corresponds to 36% of the 58 genes (Table S3D). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

bp(MESH:Aging) decreases p(FPLX:HSPA) View Subject | View Object

Ranked by decreasing median aging correlation, the induction of sHSPs and TPR genes consistently ranked high and the HSP60s, HSP40s, and HSP70s were consistently repressed. PubMed:25437566

Appears in Networks:

bp(GO:"ATP metabolic process") increases act(p(FPLX:HSPA)) View Subject | View Object

ATP hydrolysisis essential for the chaperone activity of HSP70 and HSP90, causing conformational changes that result in substrate binding (11). PubMed:25784053

Appears in Networks:

bp(MESH:Aging) decreases p(FPLX:HSPA) View Subject | View Object

Additionally, an investigation of chaperone and cochaperone gene expression in young (36±4 years of age) and aged (73 ±4 years of age) human brain tissue revealed that of 332 genes examined, 101 are significantly repressed with age, including HSP70, HSP40, HSP90, and TRiC genes (113). Furthermore, 62 chaperone genes, including several small HSPs, were found to be significantly induced, likely as a result of the cellular response to accumulating protein damage with age (113). PubMed:25784053

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

complex(p(FPLX:HSPA), p(HGNC:DNAJB1), p(HGNC:HSPH1)) hasComponent p(FPLX:HSPA) View Subject | View Object

Appears in Networks:

p(HGNC:ATXN1, var("?")) causesNoChange p(FPLX:HSPA) View Subject | View Object

Cerebellar granular neurons were found to express high levels of HSP70 in response to mHTT expression but not mAtaxin-1. PubMed:25784053

Appears in Networks:
Annotations
Cell Ontology (CL)
cerebellar granule cell

p(HGNC:HTT, var("?")) increases p(FPLX:HSPA) View Subject | View Object

Cerebellar granular neurons were found to express high levels of HSP70 in response to mHTT expression but not mAtaxin-1. PubMed:25784053

Appears in Networks:
Annotations
Cell Ontology (CL)
cerebellar granule cell

path(MESH:"Huntington Disease") positiveCorrelation p(FPLX:HSPA) View Subject | View Object

Furthermore, increased levels of HSP70 were found in the cerebellar cortex of human HD brain samples but not in tissue from unaffected individuals or from brains of PD patients (57). PubMed:25784053

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

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:

bp(GO:aging) decreases p(FPLX:HSPA) View Subject | View Object

The HSP70 and HSP40 family members exhibit significantly altered expression dynamics during aging in the human brain, both being consistently repressed with age (Brehme et al., 2014). PubMed:27491084

Appears in Networks:

bp(HBP:Proteostasis) association p(FPLX:HSPA) View Subject | View Object

Many studies based on model systems support a role for candidates from each of the major chaperome families; HSP100, HSP90, HSP70, HSP60, HSP40, sHSPs, and TPR-domain-containing proteins in proteostasis. PubMed:27491084

Appears in Networks:

bp(MESH:Aging) decreases p(FPLX:HSPA) View Subject | View Object

The HSP40, HSP60 and HSP70 families were amongst the most repressed chaperones, with HSP70s being the most repressed group overall. However, in contrast with the broad spectrum of repressed chaperone families, sHSPs and the TPR co-chaperone proteins were the only families that were significantly induced. PubMed:27491084

Appears in Networks:

p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") increases act(p(FPLX:HSPA), ma(GO:"ATPase activity")) View Subject | View Object

HSP40s play a fundamental role as part of the HSP70-HSP40 system, as co-chaperones, stimulating HSP70 ATP hydrolysis (Fig. 3) (Kampinga and Craig, 2010; Kakkar et al., 2014). PubMed:27491084

Appears in Networks:

p(UNIPROT:P32589) regulates act(p(FPLX:HSPA)) View Subject | View Object

The co- chaperone HSP40 (dHdj-1 and SIS1) and the nucleotide exchange factor SSE1 that specifically modulate HSP70 activity were also shown to suppress toxicity and aggregation in yeast and fly disease models (Chan et al., 2000; Krobitsch and Lindquist, 2000; Sadlish et al., 2008). PubMed:27491084

Appears in Networks:

a(CHEBI:ATP) regulates act(p(FPLX:HSPA)) View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

Appears in Networks:

bp(GO:"'de novo' protein folding") association act(p(FPLX:HSPA)) View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

Appears in Networks:

bp(GO:"'de novo' protein folding") association act(p(FPLX:HSPA)) View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

Appears in Networks:

bp(GO:"intracellular protein transmembrane transport") association act(p(FPLX:HSPA)) View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

Appears in Networks:

bp(GO:"protein catabolic process") association act(p(FPLX:HSPA)) View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

Appears in Networks:

bp(GO:"protein refolding") association act(p(FPLX:HSPA)) View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

Appears in Networks:

bp(GO:"protein refolding") association act(p(FPLX:HSPA)) View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

Appears in Networks:

complex(p(FPLX:"CCT_complex"), p(FPLX:HSPA)) hasComponent p(FPLX:HSPA) View Subject | View Object

Appears in Networks:

composite(p(FPLX:"CCT_complex"), p(FPLX:HSPA)) hasComponent p(FPLX:HSPA) View Subject | View Object

Appears in Networks:

composite(p(FPLX:HSP90), p(FPLX:HSPA), p(HGNC:BAG1), p(HGNC:BAG3), p(HGNC:STUB1)) hasComponent p(FPLX:HSPA) View Subject | View Object

Appears in Networks:

composite(p(FPLX:HSPA), p(HGNC:HSPH1), p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins")) hasComponent p(FPLX:HSPA) View Subject | View Object

Appears in Networks:

p(HGNCGENEFAMILY:"DNAJ (HSP40) heat shock proteins") regulates act(p(FPLX:HSPA)) View Subject | View Object

Hsp40 ( J protein) and NEF cochaperones regulate the Hsp70 reaction cy- cle (38, 100). PubMed:23746257

Appears in Networks:

p(FPLX:RAPGEF) regulates act(p(FPLX:HSPA)) View Subject | View Object

Hsp40 ( J protein) and NEF cochaperones regulate the Hsp70 reaction cy- cle (38, 100). PubMed:23746257

Appears in Networks:

Out-Edges 31

act(p(FPLX:HSPA)) association a(CHEBI:ATP) View Subject | View Object

The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566

Appears in Networks:

p(FPLX:HSPA) increases complex(p(HGNC:ATXN3, frag("?")), p(HGNC:PRKN)) View Subject | View Object

The affinity of the polyglutamine fragment to Parkin was increased by Hsp70, in agreement with the hypothesis that molecular chaperones may play a role in the recruitment of misfolded proteins to the conjugation machinery (see, for example, Bercovich et al., 1997). PubMed:14556719

Appears in Networks:

p(FPLX:HSPA) increases a(HBP:"protein aggregates") View Subject | View Object

Overexpression of the chaperone HSP70 has been found to reduce aggregate formation and death in nonneuronal cultured cells expressing mutant SOD1 (Bruening et al.,1999). PubMed:14556719

Appears in Networks:

p(FPLX:HSPA) increases bp(GO:"cell death") View Subject | View Object

Overexpression of the chaperone HSP70 has been found to reduce aggregate formation and death in nonneuronal cultured cells expressing mutant SOD1 (Bruening et al.,1999). PubMed:14556719

Appears in Networks:

p(FPLX:HSPA) isA a(MESH:"Molecular Chaperones") View Subject | View Object

Appears in Networks:

p(FPLX:HSPA) regulates bp(GO:"protein folding") View Subject | View Object

As such, HSP70 and HSP90 are central to the process of triaging proteins for refolding or elimination. PubMed:25784053

Appears in Networks:

p(FPLX:HSPA) regulates bp(MESH:Proteolysis) View Subject | View Object

As such, HSP70 and HSP90 are central to the process of triaging proteins for refolding or elimination. PubMed:25784053

Appears in Networks:

p(FPLX:HSPA) positiveCorrelation path(MESH:"Huntington Disease") View Subject | View Object

Furthermore, increased levels of HSP70 were found in the cerebellar cortex of human HD brain samples but not in tissue from unaffected individuals or from brains of PD patients (57). PubMed:25784053

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

p(FPLX:HSPA) increases deg(a(CHEBI:"amyloid-beta")) View Subject | View Object

Exercise training can increase extracellular Aβ clearance in the brains of Tg2576 mice in a dose-dependent manner through up-regulating NEP, IDE, MMP9, LRP1, and HSP70 (Moore et al. 2016) PubMed:29626319

Appears in Networks:

p(FPLX:HSPA) association bp(HBP:Proteostasis) View Subject | View Object

Many studies based on model systems support a role for candidates from each of the major chaperome families; HSP100, HSP90, HSP70, HSP60, HSP40, sHSPs, and TPR-domain-containing proteins in proteostasis. PubMed:27491084

Appears in Networks:

p(FPLX:HSPA) decreases p(HBP:"huntingtin aggregates") View Subject | View Object

In a yeast model expressing the N-terminal fragment of a polyQ-containing huntingtin protein, overexpression of the yeast HSP70 (SSA1) reduced aggregate formation, whereas the dominant-negative version of the fly homolog to HSPA1L, Hsc4-K71S, enhanced neurodegeneration (Warrick et al., 1999;) PubMed:27491084

Appears in Networks:

p(FPLX:HSPA) decreases path(MESH:"Protein Aggregation, Pathological") View Subject | View Object

These studies revealed that an increase in levels of HSP70 reduced aggregation of disease-associated proteins, thus playing a neuroprotective role. PubMed:27491084

Appears in Networks:

p(FPLX:HSPA) increases bp(GO:"'de novo' protein folding") View Subject | View Object

HSP70s function in a variety of basic cellular quality control and maintenance processes, such as proper folding of newly synthesized proteins, along with preventing protein misfolding and aggregation through the binding of exposed hydrophobic residues. PubMed:27491084

Appears in Networks:

p(FPLX:HSPA) decreases bp(HBP:misfolding) View Subject | View Object

HSP70s function in a variety of basic cellular quality control and maintenance processes, such as proper folding of newly synthesized proteins, along with preventing protein misfolding and aggregation through the binding of exposed hydrophobic residues. PubMed:27491084

Appears in Networks:

p(FPLX:HSPA) decreases a(MESH:"Protein Aggregates") View Subject | View Object

HSP70s function in a variety of basic cellular quality control and maintenance processes, such as proper folding of newly synthesized proteins, along with preventing protein misfolding and aggregation through the binding of exposed hydrophobic residues. PubMed:27491084

Appears in Networks:

p(FPLX:HSPA) decreases a(MESH:"Protein Aggregates") View Subject | View Object

Multiple studies in model systems demonstrate that overexpression of HSP70 can reduce toxicity and protein aggregation. PubMed:27491084

Appears in Networks:

p(FPLX:HSPA) decreases path(HBP:proteotoxicity) View Subject | View Object

Although HSP70 was not identified as a modifier of α -synuclein in the screen studies we selected, directed overexpression of HSP70 has been shown to reduce α -synuclein-related proteotoxicity, supporting a central role for HSP70 in diseases of protein misfolding (Auluck et al., 2002). PubMed:27491084

Appears in Networks:

p(FPLX:HSPA) decreases path(HBP:proteotoxicity) View Subject | View Object

Multiple studies in model systems demonstrate that overexpression of HSP70 can reduce toxicity and protein aggregation. PubMed:27491084

Appears in Networks:

p(FPLX:HSPA) decreases a(HBP:"alpha-synuclein aggregates") View Subject | View Object

Although HSP70 was not identified as a modifier of α -synuclein in the screen studies we selected, directed overexpression of HSP70 has been shown to reduce α -synuclein-related proteotoxicity, supporting a central role for HSP70 in diseases of protein misfolding (Auluck et al., 2002). PubMed:27491084

Appears in Networks:

act(p(FPLX:HSPA)) association bp(GO:"'de novo' protein folding") View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

Appears in Networks:

act(p(FPLX:HSPA)) association bp(GO:"'de novo' protein folding") View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

Appears in Networks:

act(p(FPLX:HSPA)) association bp(GO:"protein refolding") View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

Appears in Networks:

act(p(FPLX:HSPA)) association bp(GO:"protein refolding") View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

Appears in Networks:

act(p(FPLX:HSPA)) association bp(GO:"intracellular protein transmembrane transport") View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

Appears in Networks:

act(p(FPLX:HSPA)) association bp(GO:"protein catabolic process") View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

Appears in Networks:

p(FPLX:HSPA) decreases a(HBP:"huntingtin aggregates") View Subject | View Object

This approach is based on multiple lines of evidence demonstrating that overexpression of chaperones such as Hsp70 and Hsp40 prevents the aggregation and toxicity of huntingtin and α-synuclein (38, 231–234). PubMed:23746257

Appears in Networks:

p(FPLX:HSPA) decreases a(HBP:"alpha-synuclein aggregates") View Subject | View Object

This approach is based on multiple lines of evidence demonstrating that overexpression of chaperones such as Hsp70 and Hsp40 prevents the aggregation and toxicity of huntingtin and α-synuclein (38, 231–234). PubMed:23746257

Appears in Networks:

p(FPLX:HSPA) increases bp(GO:"'de novo' protein folding") View Subject | View Object

HSP70 chaperones have a diverse array of cellular functions but their major role is to ensure correct folding of newly synthesized proteins and to perform the refolding of proteins that are misfolded and/or aggregated. PubMed:24563850

Appears in Networks:

p(FPLX:HSPA) increases bp(GO:"protein folding") View Subject | View Object

HSP70 chaperones have a diverse array of cellular functions but their major role is to ensure correct folding of newly synthesized proteins and to perform the refolding of proteins that are misfolded and/or aggregated. PubMed:24563850

Appears in Networks:

p(FPLX:HSPA) decreases bp(HBP:misfolding) View Subject | View Object

HSP70 chaperones have a diverse array of cellular functions but their major role is to ensure correct folding of newly synthesized proteins and to perform the refolding of proteins that are misfolded and/or aggregated. PubMed:24563850

Appears in Networks:

p(FPLX:HSPA) decreases path(MESH:"Protein Aggregation, Pathological") View Subject | View Object

HSP70 chaperones have a diverse array of cellular functions but their major role is to ensure correct folding of newly synthesized proteins and to perform the refolding of proteins that are misfolded and/or aggregated. 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.