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Related Experiment Video

Updated: May 23, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

Hsp90: A means to an end.

Katie M Whalen¹, Brian C Freeman¹

¹Department of Cell and Developmental Biology, School of Molecular and Cellular Biology, University of Illinois-Urbana-Champaign, Urbana, IL 61801, USA.

Cell Stress & Chaperones

|May 21, 2026

Summary

Heat Shock Protein 90 (Hsp90) acts as a crucial gatekeeper in cellular protein quality control, influencing protein folding, maturation, and degradation. Understanding Hsp90

Area of Science:

Molecular Biology
Cellular Biology
Biochemistry

Background:

Heat Shock Protein 90 (Hsp90) is central to maintaining protein homeostasis (proteostasis) within cells.
Hsp90 functions as a gatekeeper in the cellular protein quality control pathway, influencing folding, maturation, and degradation.
The precise mechanisms by which Hsp90 directs client proteins through quality control decisions remain incompletely understood.

Purpose of the Study:

To elucidate the role of Hsp90 in linking polypeptide biogenesis with protein triage decisions.
To investigate the regulatory events governing the protein quality control decision route.
To explore the therapeutic potential of exploiting Hsp90's interaction with proteolysis pathways.

Main Methods:

Exploration of Hsp90's involvement in nascent polypeptide folding and client maturation.

Keywords:

Hsp90 Molecular chaperone Proteolysis Proteostasis

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Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

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Last Updated: May 23, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

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Published on: March 31, 2022

Analysis of modifications to the Hsp90 amino-terminal ATP-binding domain.

Investigation of Hsp90's connections to cellular proteolysis pathways.

Main Results:

Modifications to the Hsp90 ATP-binding domain can promote client protein degradation.
Hsp90 inhibitors can trigger the breakdown of clinically significant proteins.
Hsp90 plays a critical role in directing proteins towards either maintenance or degradation.

Conclusions:

Hsp90 is a key regulator of protein triage, influencing the fate of cellular proteins.
Targeting Hsp90's interaction with proteolysis pathways offers a promising therapeutic strategy.
Further understanding of Hsp90's gatekeeper function is crucial for developing novel treatments.