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p(HGNC:STUB1)

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Entity

Name
STUB1
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 13

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

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

Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease v1.0.0

Tau degradation: the ubiquitin-proteasome system versus the autophagy-lysosome system. v1.0.0

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

Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies v1.0.0

TAU and Interaction Partners v1.2.5

TAU Interactions Section of NESTOR

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

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

The Ubiquitin–Proteasome System and the Autophagic–Lysosomal System in Alzheimer Disease v1.0.0

Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0

Carboxy terminus heat shock protein 70 interacting protein reduces tau-associated degenerative changes v1.0.0

Tau in physiology and pathology v1.0.0

In-Edges 41

complex(p(HGNC:PSMD2), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:PRKN), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(p(FPLX:HSP90), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:BAG2), p(HGNC:HSPA8), p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family")) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family")) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family"), p(INTERPRO:"Heat shock protein Hsp90 family")) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:HSPA8), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

composite(p(HGNC:HSPA8), p(HGNC:STUB1), p(HGNC:UBE2D2)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

path(MESH:"Neurodegenerative Diseases") association p(HGNC:STUB1) View Subject | View Object

Several E3 Ub ligases, such as CHIP, Parkin, RNF182, may have roles in AD and other neurodegenerative diseases (Shimura et al., 2004; Khandelwal et al., 2011; Lei et al., 2012). PubMed:23528736

Appears in Networks:

complex(a(CHEBI:polypeptide), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

p(FPLX:HSP90) increases act(p(HGNC:STUB1)) View Subject | View Object

Alternatively, either Hsp70 or Hsp90 can recruit the ubiquitin E3 ligase, C-terminal Hsp70 interacting protein (CHIP), to degrade the bound substrate [104] PubMed:21882945

Appears in Networks:

complex(a(MESH:Proteins), p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family")) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

p(INTERPRO:"Heat shock protein 70 family") increases act(p(HGNC:STUB1)) View Subject | View Object

Alternatively, either Hsp70 or Hsp90 can recruit the ubiquitin E3 ligase, C-terminal Hsp70 interacting protein (CHIP), to degrade the bound substrate [104] PubMed:21882945

Appears in Networks:

p(HGNC:BAG2) decreases act(p(HGNC:STUB1)) View Subject | View Object

For example, BAG-2 inhibits client ubiquitination by CHIP by interfering with the interaction between CHIP and E2 ubiquitin-conjugating enzymes [148]. PubMed:21882945

Appears in Networks:

complex(p(HGNC:STUB1), p(HGNC:UBA2)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

path(MESH:"Alzheimer Disease") association p(HGNC:STUB1) View Subject | View Object

CHIP has been linked to several neurodegenerative disorders including Huntington’s disease, Parkinson’s disease and AD as well as other diseases such as cystic fibrosis and cancer (Dickey et al., 2007b; Edkins, 2015). PubMed:29311797

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

path(MESH:"Cystic Fibrosis") association p(HGNC:STUB1) View Subject | View Object

CHIP has been linked to several neurodegenerative disorders including Huntington’s disease, Parkinson’s disease and AD as well as other diseases such as cystic fibrosis and cancer (Dickey et al., 2007b; Edkins, 2015). PubMed:29311797

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

path(MESH:"Huntington Disease") association p(HGNC:STUB1) View Subject | View Object

CHIP has been linked to several neurodegenerative disorders including Huntington’s disease, Parkinson’s disease and AD as well as other diseases such as cystic fibrosis and cancer (Dickey et al., 2007b; Edkins, 2015). PubMed:29311797

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

path(MESH:"Parkinson Disease") association p(HGNC:STUB1) View Subject | View Object

CHIP has been linked to several neurodegenerative disorders including Huntington’s disease, Parkinson’s disease and AD as well as other diseases such as cystic fibrosis and cancer (Dickey et al., 2007b; Edkins, 2015). PubMed:29311797

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

path(MESH:Neoplasms) association p(HGNC:STUB1) View Subject | View Object

CHIP has been linked to several neurodegenerative disorders including Huntington’s disease, Parkinson’s disease and AD as well as other diseases such as cystic fibrosis and cancer (Dickey et al., 2007b; Edkins, 2015). PubMed:29311797

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

complex(p(HGNC:BAG1), p(HGNC:MAPT), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:MAPT, pmod(Ph)), p(HGNC:STUB1), p(HGNC:UBE2D2)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

a(HBP:"Tau epitope, 12E8") negativeCorrelation act(p(HGNC:STUB1)) View Subject | View Object

In particular, previous studies have demonstrated that the tau ubiquitin ligase, CHIP, is unable to bind and ubiquitinate tau species phosphorylated by Par-1/MARK2 on the 12E8 epitope (S262/356) [33], a p-tau species that is also resistant to degradation upon treatment with Hsp90 inhibitors [32,33]. Tau phosphorylated at the PHF1 epitope (S396/404) is still susceptible to degradation following Hsp90 inhibition and actually exhibits an enhanced interaction with Hsp90 PubMed:25031639

Appears in Networks:

p(HBP:"APP, ACR") association p(HGNC:STUB1) View Subject | View Object

the ACR (APP cytosolic region) interacts with the E3 ubiquitin-protein ligases Stub1, which binds the NH2 terminus of the ACR, and CRL4(CRBN), which is formed by Cul4a/b, Ddb1, and Crbn, and interacts with the COOH terminus of the ACR via Crbn. PubMed:27325702

Appears in Networks:

complex(p(HGNC:HSPA8), p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) 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(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(a(MESH:"HSP70 Heat-Shock Proteins"), p(FPLX:HSP90), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(p(FPLX:HSP90), p(HGNC:STUB1), p(MESH:Proteins, pmod(HBP:misfolded))) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(p(HBP:"Tau C3"), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(a(MESH:"HSP70 Heat-Shock Proteins"), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(a(MESH:"HSP70 Heat-Shock Proteins"), p(HGNC:STUB1), p(MESH:Proteins, pmod(HBP:misfolded))) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

p(HBP:"Tau C3") negativeCorrelation p(HGNC:STUB1) View Subject | View Object

Recent data suggest that caspases are involved in the accumulation of tau pathology [10, 25, 26], and reductions in CHIP have been shown to cause caspase activation and increased caspase-cleaved tau levels [19]. PubMed:25374103

Appears in Networks:

complex(p(HBP:"Tau isoform F (441 aa)"), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:HSPA8), p(HGNC:MAPT, pmod(Ub)), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:STUB1), p(INTERPRO:"U box domain")) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

composite(p(HBP:"4R tau", var("p.Lys280del")), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

composite(p(HBP:"Tau C3"), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

composite(p(HBP:"Tau isoform F (441 aa)"), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

act(p(FPLX:Caspase)) negativeCorrelation p(HGNC:STUB1) View Subject | View Object

Recent data suggest that caspases are involved in the accumulation of tau pathology [10, 25, 26], and reductions in CHIP have been shown to cause caspase activation and increased caspase-cleaved tau levels [19]. PubMed:25374103

Appears in Networks:

complex(p(HGNC:MAPT), p(HGNC:STUB1)) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

Out-Edges 39

p(HGNC:STUB1) increases complex(p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family"), p(INTERPRO:"Heat shock protein Hsp90 family")) View Subject | View Object

Two subnetworks emerged within this central network, corresponding to known Hsp90 and Hsp70 chaperone complexes (Figure 2, blue and orange squares, respectively). These two subnetworks were bridged by a unique set of cochaperones (Figure 2, tan squares). Among these were the wellknown bridging factors HOP/STIP1, TPR2/DNAJC7, and CHIP/ STUB1, validating our approach (Brychzy et al., 2003; Schmid et al., 2012; Xu et al., 2002). Other bridging factors in this first tier of organization included members of the Hsp40 chaperone family (DNAJB1 and DNAJB6), HSP70-binding protein 1 (HSPBP1), the TPR domain protein EDRF1, and the E3 ligase NRDP1/RNF41 PubMed:25036637

Appears in Networks:

p(HGNC:STUB1) directlyIncreases complex(p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family")) View Subject | View Object

CHIP binds Hsp90 and Hsp70 with similar affinities and can regulate the degradation of chaperone clients (Kundrat and Regan, 2010). PubMed:25036637

Appears in Networks:

p(HGNC:STUB1) directlyIncreases complex(p(FPLX:HSP90), p(HGNC:STUB1)) View Subject | View Object

CHIP binds Hsp90 and Hsp70 with similar affinities and can regulate the degradation of chaperone clients (Kundrat and Regan, 2010). PubMed:25036637

Appears in Networks:

p(HGNC:STUB1) regulates bp(GO:"cellular protein catabolic process") View Subject | View Object

CHIP binds Hsp90 and Hsp70 with similar affinities and can regulate the degradation of chaperone clients (Kundrat and Regan, 2010). PubMed:25036637

Appears in Networks:

p(HGNC:STUB1) increases p(HGNC:MAPT, pmod(Ub)) View Subject | View Object

However, another study, also using HEK cells and ubiquitin K48 and K63 mutants, demonstrated that in the presence of the E3 ligase CHIP, tau could be ubiquitylated by both K48 and K63 linkages (100). The likelihood that in vivo tau can be ubiquitylated in multiple ways is supported by studies showing tau isolated from NFTs in human brain has several forms of ubiquitin linkages as well as mono-ubiquitylation (101, 102). These data suggest that the physical structure of the ubiquitin chain is unlikely to be a sufficient signal for selectively targeting tau to either the proteasome or autophagy. PubMed:24027553

Appears in Networks:
Annotations
Text Location
Review

p(HGNC:STUB1) association path(MESH:"Neurodegenerative Diseases") View Subject | View Object

Several E3 Ub ligases, such as CHIP, Parkin, RNF182, may have roles in AD and other neurodegenerative diseases (Shimura et al., 2004; Khandelwal et al., 2011; Lei et al., 2012). PubMed:23528736

Appears in Networks:

act(p(HGNC:STUB1)) increases bp(GO:"protein catabolic process") View Subject | View Object

Alternatively, either Hsp70 or Hsp90 can recruit the ubiquitin E3 ligase, C-terminal Hsp70 interacting protein (CHIP), to degrade the bound substrate [104] PubMed:21882945

Appears in Networks:

act(p(HGNC:STUB1)) increases bp(GO:"protein ubiquitination") View Subject | View Object

For example, BAG-2 inhibits client ubiquitination by CHIP by interfering with the interaction between CHIP and E2 ubiquitin-conjugating enzymes [148]. PubMed:21882945

Appears in Networks:

p(HGNC:STUB1) association path(MESH:"Huntington Disease") View Subject | View Object

CHIP has been linked to several neurodegenerative disorders including Huntington’s disease, Parkinson’s disease and AD as well as other diseases such as cystic fibrosis and cancer (Dickey et al., 2007b; Edkins, 2015). PubMed:29311797

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

p(HGNC:STUB1) association path(MESH:"Parkinson Disease") View Subject | View Object

CHIP has been linked to several neurodegenerative disorders including Huntington’s disease, Parkinson’s disease and AD as well as other diseases such as cystic fibrosis and cancer (Dickey et al., 2007b; Edkins, 2015). PubMed:29311797

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

p(HGNC:STUB1) association path(MESH:"Alzheimer Disease") View Subject | View Object

CHIP has been linked to several neurodegenerative disorders including Huntington’s disease, Parkinson’s disease and AD as well as other diseases such as cystic fibrosis and cancer (Dickey et al., 2007b; Edkins, 2015). PubMed:29311797

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

p(HGNC:STUB1) association path(MESH:"Cystic Fibrosis") View Subject | View Object

CHIP has been linked to several neurodegenerative disorders including Huntington’s disease, Parkinson’s disease and AD as well as other diseases such as cystic fibrosis and cancer (Dickey et al., 2007b; Edkins, 2015). PubMed:29311797

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

p(HGNC:STUB1) association path(MESH:Neoplasms) View Subject | View Object

CHIP has been linked to several neurodegenerative disorders including Huntington’s disease, Parkinson’s disease and AD as well as other diseases such as cystic fibrosis and cancer (Dickey et al., 2007b; Edkins, 2015). PubMed:29311797

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

p(HGNC:STUB1) increases deg(p(HGNC:MAPT, pmod(Ph))) View Subject | View Object

In tauopathic mice, CHIP regulates the removal of tau species that have undergone abnormal phosphorylation and folding (Dickey et al., 2007b). PubMed:29311797

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

p(HGNC:STUB1) increases deg(p(HGNC:MAPT, pmod(HBP:misfolding))) View Subject | View Object

In tauopathic mice, CHIP regulates the removal of tau species that have undergone abnormal phosphorylation and folding (Dickey et al., 2007b). PubMed:29311797

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

p(HGNC:STUB1) isA complex(p(HGNC:MAPT, pmod(Ph)), p(HGNC:STUB1), p(HGNC:UBE2D2)) View Subject | View Object

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p(HGNC:STUB1) isA complex(p(HGNC:BAG1), p(HGNC:MAPT), p(HGNC:STUB1)) View Subject | View Object

Appears in Networks:

act(p(HGNC:STUB1)) negativeCorrelation a(HBP:"Tau epitope, 12E8") View Subject | View Object

In particular, previous studies have demonstrated that the tau ubiquitin ligase, CHIP, is unable to bind and ubiquitinate tau species phosphorylated by Par-1/MARK2 on the 12E8 epitope (S262/356) [33], a p-tau species that is also resistant to degradation upon treatment with Hsp90 inhibitors [32,33]. Tau phosphorylated at the PHF1 epitope (S396/404) is still susceptible to degradation following Hsp90 inhibition and actually exhibits an enhanced interaction with Hsp90 PubMed:25031639

Appears in Networks:

act(p(HGNC:STUB1)) increases deg(p(HGNC:MAPT)) View Subject | View Object

In particular, previous studies have demonstrated that the tau ubiquitin ligase, CHIP, is unable to bind and ubiquitinate tau species phosphorylated by Par-1/MARK2 on the 12E8 epitope (S262/356) [33], a p-tau species that is also resistant to degradation upon treatment with Hsp90 inhibitors [32,33]. Tau phosphorylated at the PHF1 epitope (S396/404) is still susceptible to degradation following Hsp90 inhibition and actually exhibits an enhanced interaction with Hsp90 PubMed:25031639

Appears in Networks:

p(HGNC:STUB1) association p(HBP:"APP, ACR") View Subject | View Object

the ACR (APP cytosolic region) interacts with the E3 ubiquitin-protein ligases Stub1, which binds the NH2 terminus of the ACR, and CRL4(CRBN), which is formed by Cul4a/b, Ddb1, and Crbn, and interacts with the COOH terminus of the ACR via Crbn. PubMed:27325702

Appears in Networks:

p(HGNC:STUB1) isA complex(GO:"ubiquitin ligase complex") View Subject | View Object

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p(HGNC:STUB1) decreases path(HP:Neurodegeneration) View Subject | View Object

For example, overexpression of the human TPR domain-containing co- chaperone CHIP suppresses neurodegeneration in fly models expressing polyQ-containing versions of ataxin 1 and the N-terminal huntingtin fragment (Al-Ramahi et al., 2006). PubMed:27491084

Appears in Networks:

p(HGNC:STUB1) increases complex(p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)), p(HGNC:STUB1)) View Subject | View Object

On the other hand, it has been reported that the E3 ligase CHIP (carboxyl terminus of the Hsc70-interacting protein) binds to tau and is involved in the degradation of abnormal forms of tau, including insoluble tau and hyperphosphorylated tau, coordinately with Hsp70 (Petrucelli et al. 2004; Dickey et al. 2006). PubMed:22908190

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p(HGNC:STUB1) regulates act(p(HGNC:CASP3)) View Subject | View Object

CHIP is also implicated in regulation of Caspase 3 activity PubMed:25374103

Appears in Networks:

p(HGNC:STUB1) increases complex(p(HBP:"Tau C3"), p(HGNC:STUB1)) View Subject | View Object

CHIP interacts more strongly with tauΔC than full-length tau [18], suggesting it is involved in caspase cleaved tau degradation PubMed:25374103

Appears in Networks:

p(HGNC:STUB1) increases deg(p(HGNC:MAPT, pmod(HBP:hyperphosphorylation))) View Subject | View Object

Recent data suggest that a critical mediator of refolding or clearance of hyperphosphorylated tau is via the HSP70/HSP90 heat shock pathways in which a specific E3 ubiquitin ligase, CHIP (carboxy terminus Hsp70 interacting protein), can recognize and target for degradation abnormal but not normal tau molecules [14–16]. PubMed:25374103

Appears in Networks:

p(HGNC:STUB1) increases complex(p(HBP:"Tau C3"), p(HGNC:STUB1)) View Subject | View Object

Dolan et al. [20] showed that CHIP interacts more strongly with tauC3 than full length tau. PubMed:25374103

Appears in Networks:

p(HGNC:STUB1) increases deg(p(HBP:"Tau C3")) View Subject | View Object

CHIP interacts more strongly with tauΔC than full-length tau [18], suggesting it is involved in caspase cleaved tau degradation PubMed:25374103

Appears in Networks:

p(HGNC:STUB1) negativeCorrelation p(HBP:"Tau C3") View Subject | View Object

Recent data suggest that caspases are involved in the accumulation of tau pathology [10, 25, 26], and reductions in CHIP have been shown to cause caspase activation and increased caspase-cleaved tau levels [19]. PubMed:25374103

Appears in Networks:

p(HGNC:STUB1) increases deg(p(HBP:"Tau C3")) View Subject | View Object

These results indicate that CHIP is involved in degradation of caspases and caspase-cleaved tau. PubMed:25374103

Appears in Networks:

p(HGNC:STUB1) causesNoChange bp(GO:"cell death") View Subject | View Object

Toxicity assays revealed that neither CHIP nor any of the tau constructs caused cell death compared to the control GFP vector (Supplementary Fig. 1). PubMed:25374103

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p(HGNC:STUB1) increases complex(p(FPLX:HSP90), p(HGNC:STUB1)) View Subject | View Object

The co-chaperone CHIP interacts with Hsp70/Hsp90 to bind unfolded and misfolded proteins PubMed:25374103

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p(HGNC:STUB1) increases complex(a(MESH:"HSP70 Heat-Shock Proteins"), p(HGNC:STUB1)) View Subject | View Object

The co-chaperone CHIP interacts with Hsp70/Hsp90 to bind unfolded and misfolded proteins PubMed:25374103

Appears in Networks:

p(HGNC:STUB1) increases complex(p(HGNC:HSPA8), p(HGNC:MAPT, pmod(Ub)), p(HGNC:STUB1)) View Subject | View Object

Either of these domains could be critical for degradation of tau since ubiquitination targets proteins for degradation and CHIP is known to interact with full-length tau in a complex with Hsc70/Hsp70 and poly-ubiquitinated tau [17]. PubMed:25374103

Appears in Networks:

p(HGNC:STUB1) increases deg(p(HBP:"4R tau", var("p.Lys280del"))) View Subject | View Object

After cyclohexamide treatment, we could still detect a significant decrease in tau levels in cells that were co-transfected with CHIP indicating that the reduction in tau levels due to CHIP is due to degradation and not to transcriptional down-regulation (Supplementary Fig. 3). PubMed:25374103

Appears in Networks:

p(HGNC:STUB1) negativeCorrelation act(p(FPLX:Caspase)) View Subject | View Object

Recent data suggest that caspases are involved in the accumulation of tau pathology [10, 25, 26], and reductions in CHIP have been shown to cause caspase activation and increased caspase-cleaved tau levels [19]. PubMed:25374103

Appears in Networks:

p(HGNC:STUB1) increases deg(p(FPLX:Caspase)) View Subject | View Object

These results indicate that CHIP is involved in degradation of caspases and caspase-cleaved tau. PubMed:25374103

Appears in Networks:

p(HGNC:STUB1) increases complex(p(HBP:"Tau isoform F (441 aa)"), p(HGNC:STUB1)) View Subject | View Object

Dolan et al. [20] showed that CHIP interacts more strongly with tauC3 than full length tau. PubMed:25374103

Appears in Networks:

p(HGNC:STUB1) increases p(HGNC:MAPT, pmod(UbK48)) View Subject | View Object

Tau is known to be ubiquitylated through Lys48 linkages by CHIP for proteasomal degradation PubMed:26631930

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.