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Updated: Apr 28, 2026
Mapping Dysfunctional Protein-Protein Interactions in Disease
Published on: October 24, 2025
Affinity purification probes of potential use to investigate the endogenous Hsp70 interactome in cancer
Anna Rodina1, Tony Taldone, Yanlong Kang
1Program in Molecular Pharmacology and Chemistry and Department of Medicine and §Program in Molecular Biology, Proteomics Core, Memorial Sloan-Kettering Cancer Center , New York, New York 10021, United States.
Abstract:
Heat shock protein 70 (Hsp70) is a family of proteins with key roles in regulating malignancy. Cancer cells rely on Hsp70 to inhibit apoptosis, regulate senescence and autophagy, and maintain the stability of numerous onco-proteins. Despite these important biological functions in cancer, robust chemical tools that enable the analysis of the Hsp70-regulated proteome in a tumor-by-tumor manner are yet unavailable. Here we take advantage of a recently reported Hsp70 ligand to design and develop an affinity purification chemical toolset for potential use in the investigation of the endogenous Hsp70-interacting proteome in cancer. We demonstrate that these tools lock Hsp70 in complex with onco-client proteins and effectively isolate Hsp70 complexes for identification through biochemical techniques. Using these tools we provide proof-of-concept analyses that glimpse into the complex roles played by Hsp70 in maintaining a multitude of cell-specific malignancy-driving proteins.
Insights
Researchers developed novel chemical tools to study Heat Shock Protein 70 (Hsp70) interactions in cancer. These tools help identify Hsp70-regulated proteins crucial for tumor growth and survival.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Heat shock protein 70 (Hsp70) is vital for cancer cell survival, regulating apoptosis, senescence, and autophagy.
- Hsp70 stabilizes numerous oncoproteins, contributing significantly to malignancy.
- Current methods lack tools for analyzing the Hsp70-regulated proteome on a tumor-specific basis.
Purpose of the Study:
- To design and develop chemical tools for investigating the endogenous Hsp70-interacting proteome in cancer.
- To enable tumor-by-tumor analysis of Hsp70's role in malignancy.
Main Methods:
- Leveraged a known Hsp70 ligand to create an affinity purification chemical toolset.
- Demonstrated the tools' ability to lock Hsp70 with onco-client proteins.
- Utilized biochemical techniques for identifying isolated Hsp70 complexes.
Main Results:
- Developed and validated novel chemical tools for Hsp70 proteome analysis.
- Showcased the tools' efficacy in capturing Hsp70-oncoprotein interactions.
- Provided proof-of-concept for analyzing Hsp70's role in maintaining malignancy-driving proteins.
Conclusions:
- The developed chemical toolset facilitates the study of the Hsp70 interactome in cancer.
- These tools offer new avenues for understanding Hsp70's multifaceted roles in tumor progression.
- Enables detailed investigation into cell-specific Hsp70-dependent malignancy mechanisms.
