Related Experiment Video

Updated: Jun 19, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

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

Published on: July 21, 2021

The Hsp90 chaperone machinery: from structure to drug development

Ji-Sook Hahn1

  • 1School of Chemical and Biological Engineering, Seoul National University, Seoul 151-744, Korea. hahnjs@snu.ac.kr

BMB Reports
|October 31, 2009
PubMed

Insights

Heat shock protein 90 (Hsp90) is crucial for cancer cell survival. Understanding its co-chaperones and ATPase cycle is key to developing new anti-cancer drugs targeting Hsp90.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cancer Research

Background:

  • Heat shock protein 90 (Hsp90) is a molecular chaperone essential for cellular processes.
  • Hsp90 is vital for stabilizing oncoproteins, making it critical for cancer cell malignancy.
  • Hsp90's role in client protein recognition remains incompletely understood.

Purpose of the Study:

  • To review the regulatory roles of Hsp90 co-chaperones in the Hsp90 ATPase cycle.
  • To explore how co-chaperones influence Hsp90's selection of client proteins.
  • To discuss the development of Hsp90 inhibitors based on structural insights.

Main Methods:

  • Literature review of structural studies on Hsp90.
  • Analysis of Hsp90 co-chaperone interactions.
  • Examination of Hsp90 ATPase activity regulation.

Main Results:

  • Hsp90 co-chaperones significantly regulate the Hsp90 ATPase cycle.
  • Co-chaperones play a critical role in determining Hsp90 client protein specificity.
  • Structural studies provide a basis for designing targeted Hsp90 inhibitors.

Conclusions:

  • Hsp90 co-chaperones are key regulators of Hsp90 function and client interaction.
  • Targeting the Hsp90 machinery offers a promising strategy for cancer therapy.
  • Further structural and mechanistic studies will advance Hsp90-targeted drug development.

More Related Videos

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors07:57

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

Published on: January 20, 2023

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology09:39

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

Published on: March 31, 2022

Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Drug Discovery: Overview01:26

Drug Discovery: Overview

Drug discovery is a multifaceted process involving extensive screening, testing, and optimization of lead compounds to identify potential new drugs for therapeutic use. It combines several approaches, including screening large numbers of natural products, chemical modification of known active molecules, identification of new drug targets, and rational design based on biological mechanisms and drug-receptor structure. These approaches are carried out in both academic research laboratories and...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...