Target intelligence / Profile preview

Heat shock protein HSP 90-beta (Hsp90β)

Target
Hsp90β
Molecular classification
Molecular chaperone, Heat Shock Protein
01

Overview

Heat shock protein HSP 90-beta (Hsp90β) is a constitutively expressed molecular chaperone found in the cytoplasm of eukaryotic cells. It is one of two major cytoplasmic isoforms of HSP90 in vertebrates. Hsp90β assists folding, stabilization, activation, and assembly/disassembly of many client proteins and maintains cellular homeostasis by preventing aggregation/misfolding. Dysregulation or overexpression is implicated in various diseases, particularly cancer, where it supports the stability and functionality of mutated oncoproteins. Inhibitors targeting its ATPase activity are being developed as potential therapeutics.

02

Mechanism of action

Inhibition of ATPase activity leading to destabilization of client oncoproteins.

03

Biological functions

Protein foldingProtein stabilizationProtein assembly/disassemblyCell cycle controlSignal transductionApoptosis regulationProtein quality controlMaintaining cellular homeostasis
04

Disease associations

CancerNeurodegenerative diseaseCataractsInfectious diseases
05

Safety considerations

Potential for broad effects due to interaction with numerous client proteins.Development of resistance to inhibitors.
06

Interacting drugs

Hsp90 inhibitors (targeting ATPase activity)

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