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A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways 1.0.0

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charles.hoyt@scai.fraunhofer.de at 2019-02-27 16:21:27.633185
Authors
Sandra Spalek
Contact
charles.hoyt@scai.fraunhofer.de
License
CC BY 4.0
Copyright
Copyright © 2018 Fraunhofer Institute SCAI, All rights reserved.
Number Nodes
274
Number Edges
533
Number Components
8
Network Density
0.00712547792839764
Average Degree
1.94525547445255
Number Citations
1
Number BEL Errors
0

Content Statistics

Network Overlap

The node-based overlap between this network and other networks is calculated as the Szymkiewicz-Simpson coefficient of their respective nodes. Up to the top 10 are shown below.

Network Overlap
Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0 16%
Protein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition v1.0.0 15%
Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity v1.0.0 15%
Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0 14%
A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease. v1.0.0 14%
Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies v1.0.0 14%
Carboxy terminus heat shock protein 70 interacting protein reduces tau-associated degenerative changes v1.0.0 8%
TAU and Interaction Partners v1.2.5 7%
Tau degradation: the ubiquitin-proteasome system versus the autophagy-lysosome system. v1.0.0 7%
Perilous journey: a tour of the ubiquitin–proteasome system v1.0.0 5%

Sample Edges

a(GO:"COPI-coated vesicle") regulates bp(GO:"retrograde transport, vesicle recycling within Golgi") View Subject | View Object

However, AP-MS and LUMIER revealed that it did interact strongly with multiple DEAH/DEAD box RNA helicases and several subunits of the COPI complex, which regulates retrograde signaling between Golgi compartments (Figures 2 and 6E) PubMed:25036637

a(HBP:"OSW-1") decreases complex(p(HGNC:FKBP6), p(HGNC:OSBP)) View Subject | View Object

Indeed, OSW-1 treatment led to the dissociation of OSBP from FKBP36 (Figure 3C) PubMed:25036637

a(MESH:"Argonaute Proteins") directlyIncreases complex(a(MESH:"Argonaute Proteins"), p(HGNC:PPP5C)) View Subject | View Object

LRR proteins interacted particularly strongly with the SGT1 cochaperone, whereas Argonaute proteins bound the protein phosphatase PP5 and p23, both of which are well-characterized Hsp90 cochaperones (Figure 6A) PubMed:25036637

a(MESH:"Argonaute Proteins") directlyIncreases complex(a(MESH:"Argonaute Proteins"), p(HGNC:PTGES3)) View Subject | View Object

LRR proteins interacted particularly strongly with the SGT1 cochaperone, whereas Argonaute proteins bound the protein phosphatase PP5 and p23, both of which are well-characterized Hsp90 cochaperones (Figure 6A) PubMed:25036637

a(PUBCHEM:23624255) decreases act(p(INTERPRO:"Heat shock protein Hsp90 family")) View Subject | View Object

Ganetespib treatment had a strong effect on most Hsp90- client interactions. Of the 630 unique proteins that we detected by LUMIER assay, 46% significantly decreased their interaction with Hsp90beta (change in LUMIER score > 1.5, adjusted p value <0.05; Figure 4A) PubMed:25036637

Sample Nodes

p(HGNC:TP53)

In-Edges: 6 | Out-Edges: 1 | Explore Neighborhood | Download JSON

p(FPLX:HSP90)

In-Edges: 82 | Out-Edges: 48 | Classes: 1 | Explore Neighborhood | Download JSON

p(HGNC:HSP90AB1)

In-Edges: 16 | Out-Edges: 6 | Explore Neighborhood | Download JSON

p(HGNC:HSPA8)

In-Edges: 25 | Out-Edges: 13 | Explore Neighborhood | Download JSON

p(HGNC:STIP1)

In-Edges: 6 | Out-Edges: 5 | Explore Neighborhood | Download JSON

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.