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Epichaperome Complex (N/A)
- Target
- N/A
- Molecular classification
- Protein Complex, Chaperone complex
01
Overview
The epichaperome is a pathologically altered protein complex formed by the assembly of chaperones, co-chaperones, and other associated factors under conditions of chronic cellular stress. It acts as a scaffolding platform for aberrant protein-protein interactions, disrupting normal cellular function and is implicated in various diseases, including cancer and neurodegenerative disorders. Unlike normal chaperone complexes, the epichaperome is long-lived and can be selectively targeted by small molecules.
- Other names
- Altered chaperone complexPathological chaperone networkStress-induced chaperone complex
02
Mechanism of action
Selective inhibition/dismantling of the epichaperome complex
03
Biological functions
Protein folding (dysregulated)Protein-protein interaction (PPI) scaffoldingStress responseCell survival (under stress)Signal transduction (altered)
04
Disease associations
CancerNeurodegenerative diseaseStress-related disorders
05
Safety considerations
Potential for off-target effects on normal chaperone functionDevelopment of resistanceComplex drug interactions due to widespread PPI rewiring
06
Interacting drugs
PU-H71
2 more in the full profile.
07
Biomarkers
Presence of epichaperome complexLevels of HSP90 and HSC70 in complexSpecific epichaperome-associated PPIs
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