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Covalently Linked Protein Regulators

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Related Experiment Video

Updated: Jul 20, 2025

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Detecting Posttranslational Modifications of Hsp90 Isoforms.

Rebecca A Sager¹, Sarah J Backe¹, Len Neckers²

¹Department of Urology, SUNY Upstate Medical University, Syracuse, NY, USA.

Methods in Molecular Biology (Clifton, N.J.)

|August 4, 2023

Summary

Heat shock protein 90 (Hsp90) is a vital molecular chaperone in eukaryotes, crucial for protein stability and regulating processes like carcinogenesis. Its function relies on ATP binding and hydrolysis, modulated by co-chaperones and post-translational modifications.

Keywords:

Heat shock protein 90 (Hsp90)Molecular chaperones O-GlcNAcylation Phosphorylation Posttranslational modification SUMOylation TRAP1 Ubiquitination

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

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Last Updated: Jul 20, 2025

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Published on: November 29, 2013

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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

Area of Science:

Molecular biology
Biochemistry
Cell biology

Background:

Heat shock protein 90 (Hsp90) is an essential eukaryotic molecular chaperone.
Hsp90 plays a critical role in stabilizing proteins involved in multistep carcinogenesis.
Hsp90 exists in various isoforms, including cytosolic Hsp90α/β, ER-localized GRP94, and mitochondrial TRAP1.

Purpose of the Study:

To investigate the fundamental role of Hsp90 as a molecular chaperone.
To explore the regulatory mechanisms of Hsp90 activity, including ATP hydrolysis.
To examine the influence of co-chaperones and post-translational modifications on Hsp90.

Main Methods:

Expression and purification of Hsp90 and TRAP1 in mammalian and yeast cells.
Detection of post-translational modifications using immunoblotting techniques.

Main Results:

Hsp90's chaperone function is intrinsically linked to its ATP-binding and hydrolysis capabilities.
Co-chaperones and post-translational modifications significantly impact Hsp90 stability and ATPase activity regulation.

Conclusions:

Hsp90 is a key regulator of protein homeostasis and cellular processes, including cancer development.
Understanding Hsp90 regulation through co-chaperones and PTMs is crucial for therapeutic targeting.