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p(FPLX:"CCT_complex")

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Entity

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

Appears in Networks 3

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

The Biology of Proteostasis in Aging and Disease v1.0.0

Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0

In-Edges 6

a(MESH:"Cellular Structures") association p(FPLX:"CCT_complex") View Subject | View Object

TRiC is essential for proper posttranslational folding of the cytoskeletal components actin and tubulin and is therefore essential for cell structure, division, and cargo delivery (11). PubMed:25784053

Appears in Networks:

a(PUBCHEM:377503130) decreases act(p(FPLX:"CCT_complex")) 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

bp(GO:"cell division") association p(FPLX:"CCT_complex") View Subject | View Object

TRiC is essential for proper posttranslational folding of the cytoskeletal components actin and tubulin and is therefore essential for cell structure, division, and cargo delivery (11). PubMed:25784053

Appears in Networks:

bp(GO:"intracellular transport") association p(FPLX:"CCT_complex") View Subject | View Object

TRiC is essential for proper posttranslational folding of the cytoskeletal components actin and tubulin and is therefore essential for cell structure, division, and cargo delivery (11). PubMed:25784053

Appears in Networks:

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

Appears in Networks:

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

Appears in Networks:

Out-Edges 7

p(FPLX:"CCT_complex") decreases a(CHEBI:"amyloid-beta polypeptide 42") View Subject | View Object

This functional screen identified 18 genes (Figure 3D), corresponding to ten ATP-dependent chaperones, HSC70 (hsp-1), HSP90 (daf-21), and eight subunits of the CCT/TRiC chaperonin complex; the co-chaperones, HSP40 (dnj-12) and CDC37 (cdc-37); and the TPR-domain pro- tein STI1 that upon knockdown significantly enhanced A b 42 pro- teotoxicity (Figure 3D). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

p(FPLX:"CCT_complex") increases a(HBP:"huntingtin aggregates") View Subject | View Object

These included all subunits of the CCT/TRiC complex (except CCT5); HSP40 and HSP70 family members DNAJA1 (HDJ-2), DNAJA4, HSPA8 (HSC70), and HSPA14 (Figures 5B and 5C); and the TPR-domain APC/C subunits CDC23 and CDC27 that, upon knockdown, led to significantly elevated aggregation (Figure S5B). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

p(FPLX:"CCT_complex") association a(MESH:"Cellular Structures") View Subject | View Object

TRiC is essential for proper posttranslational folding of the cytoskeletal components actin and tubulin and is therefore essential for cell structure, division, and cargo delivery (11). PubMed:25784053

Appears in Networks:

p(FPLX:"CCT_complex") association bp(GO:"cell division") View Subject | View Object

TRiC is essential for proper posttranslational folding of the cytoskeletal components actin and tubulin and is therefore essential for cell structure, division, and cargo delivery (11). PubMed:25784053

Appears in Networks:

p(FPLX:"CCT_complex") association bp(GO:"intracellular transport") View Subject | View Object

TRiC is essential for proper posttranslational folding of the cytoskeletal components actin and tubulin and is therefore essential for cell structure, division, and cargo delivery (11). 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

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

TRiC also interacts with N-terminal fragments of mutant huntingtin that contain an expanded polyglutamine repeat sequence (165–168). Binding to TRiC modulates the aggregation properties of this protein and reduces its cytotoxicity. PubMed:23746257

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.