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p(HGNC:HSPB1)

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Entity

Name
HSPB1
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 4

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

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

TAU and Interaction Partners v1.2.5

TAU Interactions Section of NESTOR

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

In-Edges 10

complex(p(HGNC:BAG3), p(HGNC:HSPB1)) hasComponent p(HGNC:HSPB1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:BAG4), p(HGNC:HSPB1)) hasComponent p(HGNC:HSPB1) View Subject | View Object

Appears in Networks:

bp(GO:"long-term synaptic potentiation") positiveCorrelation p(HGNC:HSPB1) View Subject | View Object

Recently, our group demonstrated that viral delivery of wild-type Hsp27 into the brains of tau-transgenic mice reduced tau levels and rescued long-term potentiation deficits. PubMed:21882945

Appears in Networks:

complex(a(MESH:"Neurofibrillary Tangles"), p(HGNC:HSPB1)) hasComponent p(HGNC:HSPB1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:HSPB1), p(HGNC:MAPT, pmod(HBP:hyperphosphorylation))) hasComponent p(HGNC:HSPB1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:HSPB1), p(HGNC:MAPT, pmod(Ph))) hasComponent p(HGNC:HSPB1) View Subject | View Object

Appears in Networks:

bp(GO:"neuron apoptotic process") negativeCorrelation p(HGNC:HSPB1) View Subject | View Object

Taken together, pathological hyperphosphorylated tau caused cell death, and Hsp27 attenuated the cell toxicity of pathological hyperphosphorylated tau. PubMed:14963027

Appears in Networks:
Annotations
Uberon
temporal cortex

p(HGNC:MAPT, pmod(Ph)) association p(HGNC:HSPB1) View Subject | View Object

Here we show that heat shock protein 27 (Hsp27) preferentially binds pathological hyperphosphorylated tau and paired helical filaments tau directly but not non-phosphorylated tau. The formation of this complex altered the conformation of pathological hyperphosphorylated tau and reduced its concentration by facilitating its degradation and dephosphorylation. PubMed:14963027

Appears in Networks:
Annotations
Uberon
temporal cortex

a(HBP:"amyloid-beta aggregates") association p(HGNC:HSPB1) View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

Appears in Networks:

path(MESH:"Alzheimer Disease") increases p(HGNC:HSPB1) View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

Appears in Networks:
Annotations
MeSH
Brain

Out-Edges 15

p(HGNC:HSPB1) increases bp(GO:"protein quality control for misfolded or incompletely synthesized proteins") View Subject | View Object

During protein quality control, Hsp70, Hsp90 and Hsp27 (and their co-chaperones) often work in concert. If prolonged misfolding is detected, the chaperones shuttle the protein to a degradation endpoint, such as the proteasome or autophagy PubMed:21882945

Appears in Networks:

p(HGNC:HSPB1) increases bp(GO:"proteasomal protein catabolic process") View Subject | View Object

During protein quality control, Hsp70, Hsp90 and Hsp27 (and their co-chaperones) often work in concert. If prolonged misfolding is detected, the chaperones shuttle the protein to a degradation endpoint, such as the proteasome or autophagy PubMed:21882945

Appears in Networks:

p(HGNC:HSPB1) increases bp(GO:autophagy) View Subject | View Object

During protein quality control, Hsp70, Hsp90 and Hsp27 (and their co-chaperones) often work in concert. If prolonged misfolding is detected, the chaperones shuttle the protein to a degradation endpoint, such as the proteasome or autophagy PubMed:21882945

Appears in Networks:

p(HGNC:HSPB1) directlyIncreases complex(p(HGNC:HSPB1), p(HGNC:MAPT, pmod(HBP:hyperphosphorylation))) View Subject | View Object

Hsp27 has emerged as a potential target for tau regulation based on early findings that it preferentially binds to phosphorylated and hyperphosphorylated tau and promotes their clearance [125,126] PubMed:21882945

Appears in Networks:

p(HGNC:HSPB1) directlyIncreases complex(p(HGNC:HSPB1), p(HGNC:MAPT, pmod(Ph))) View Subject | View Object

Hsp27 has emerged as a potential target for tau regulation based on early findings that it preferentially binds to phosphorylated and hyperphosphorylated tau and promotes their clearance [125,126] PubMed:21882945

Appears in Networks:

p(HGNC:HSPB1) increases p(HGNC:MAPT) View Subject | View Object

However, astrocyte-derived Hsp27 has been shown to promote tau accumulation and Hsp27 associates with tau tangles in a mouse model [127,128], suggesting a more complex relationship PubMed:21882945

Appears in Networks:
Annotations
Cell Ontology (CL)
astrocyte

p(HGNC:HSPB1) decreases p(HGNC:MAPT) View Subject | View Object

Recently, our group demonstrated that viral delivery of wild-type Hsp27 into the brains of tau-transgenic mice reduced tau levels and rescued long-term potentiation deficits. PubMed:21882945

Appears in Networks:

p(HGNC:HSPB1) directlyIncreases complex(a(MESH:"Neurofibrillary Tangles"), p(HGNC:HSPB1)) View Subject | View Object

However, astrocyte-derived Hsp27 has been shown to promote tau accumulation and Hsp27 associates with tau tangles in a mouse model [127,128], suggesting a more complex relationship PubMed:21882945

Appears in Networks:

p(HGNC:HSPB1) positiveCorrelation bp(GO:"long-term synaptic potentiation") View Subject | View Object

Recently, our group demonstrated that viral delivery of wild-type Hsp27 into the brains of tau-transgenic mice reduced tau levels and rescued long-term potentiation deficits. PubMed:21882945

Appears in Networks:

p(HGNC:HSPB1) decreases act(p(HGNC:MAPT, pmod(Ph))) View Subject | View Object

Taken together, pathological hyperphosphorylated tau caused cell death, and Hsp27 attenuated the cell toxicity of pathological hyperphosphorylated tau. PubMed:14963027

Appears in Networks:
Annotations
Uberon
temporal cortex

p(HGNC:HSPB1) association p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

Here we show that heat shock protein 27 (Hsp27) preferentially binds pathological hyperphosphorylated tau and paired helical filaments tau directly but not non-phosphorylated tau. The formation of this complex altered the conformation of pathological hyperphosphorylated tau and reduced its concentration by facilitating its degradation and dephosphorylation. PubMed:14963027

Appears in Networks:
Annotations
Uberon
temporal cortex

p(HGNC:HSPB1) causesNoChange p(HGNC:MAPT) View Subject | View Object

Here we show that heat shock protein 27 (Hsp27) preferentially binds pathological hyperphosphorylated tau and paired helical filaments tau directly but not non-phosphorylated tau. The formation of this complex altered the conformation of pathological hyperphosphorylated tau and reduced its concentration by facilitating its degradation and dephosphorylation. PubMed:14963027

Appears in Networks:
Annotations
Uberon
temporal cortex

p(HGNC:HSPB1) increases complex(p(HGNC:HSPB1), p(HGNC:MAPT, pmod(Ph))) View Subject | View Object

Here we show that heat shock protein 27 (Hsp27) preferentially binds pathological hyperphosphorylated tau and paired helical filaments tau directly but not non-phosphorylated tau. The formation of this complex altered the conformation of pathological hyperphosphorylated tau and reduced its concentration by facilitating its degradation and dephosphorylation. PubMed:14963027

Appears in Networks:
Annotations
Uberon
temporal cortex

p(HGNC:HSPB1) negativeCorrelation bp(GO:"neuron apoptotic process") View Subject | View Object

Taken together, pathological hyperphosphorylated tau caused cell death, and Hsp27 attenuated the cell toxicity of pathological hyperphosphorylated tau. PubMed:14963027

Appears in Networks:
Annotations
Uberon
temporal cortex

p(HGNC:HSPB1) association a(HBP:"amyloid-beta aggregates") View Subject | View Object

The importance of sHSPs in disease was originally noted from the observations that HSPB1 and CRYAB were overexpressed in AD brains (Shinohara et al., 1993; Renkawek et al., 1994a,b) and HSPB1, CRYAB, HSPB6 and HSPB8 were associated with AD plaques (Shao et al., 2012). PubMed:27491084

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.