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Related Experiment Video

Updated: Jul 13, 2026

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

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

Published on: March 31, 2022

Cdc37: a protein kinase chaperone?

T Hunter¹, R Y Poon

¹The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA.

Trends in Cell Biology

|April 1, 1997

Summary

Protein kinase activity is regulated by folding, with Cdc37 and heat-shock protein Hsp90 acting as a general chaperone. These proteins are essential for the function of diverse kinases, particularly in cell-cycle control.

Area of Science:

Molecular Biology
Cell Signaling
Protein Biochemistry

Background:

Protein kinase activity is typically regulated by phosphorylation and subunit association.
Emerging evidence highlights protein folding as a critical regulatory mechanism for kinase activation.

Purpose of the Study:

To investigate the role of protein folding in kinase regulation.
To identify key proteins involved in facilitating kinase activation through folding.

Main Methods:

The study focuses on the interaction between Cdc37, Hsp90, and various protein kinases.
Investigated the requirement of Cdc37 and Hsp90 for the activity of diverse kinases.

Main Results:

The 50-kDa protein Cdc37 and heat-shock protein Hsp90 bind to diverse protein kinases.

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

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Last Updated: Jul 13, 2026

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

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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Published on: June 7, 2018

Cdc37 and Hsp90 are required for the activity of kinases such as Cdk4, v-Src, Raf, and SEVENLESS.

These proteins may function as a general chaperone for protein kinases.

Conclusions:

Protein folding is an important regulatory mechanism for protein kinases.
Cdc37 and Hsp90 act as a general chaperone complex for protein kinases.
This chaperone activity is particularly relevant for kinases involved in signal transduction and cell-cycle control.