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Updated: Mar 25, 2026

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology
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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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Unusual Suspects in the Twilight Zone Between the Hsp90 Interactome and Carcinogenesis

Evangelia Vartholomaiou1, Pablo C Echeverría1, Didier Picard1

  • 1Département de Biologie Cellulaire, Université de Genève, Sciences III, Geneva, Switzerland.

Advances in Cancer Research
|February 27, 2016
PubMed

Insights

Cancer cells are more sensitive to Hsp90 inhibition due to proteostasis issues. This review explores understudied Hsp90 clients as potential cancer therapeutic targets.

Area of Science:

  • Oncology
  • Molecular Biology
  • Biochemistry

Background:

  • The molecular chaperone Hsp90 is crucial for protein folding and stability.
  • Cancer cells exhibit heightened sensitivity to Hsp90 inhibition compared to normal cells.
  • This sensitivity is linked to increased Hsp90 dependence, aneuploidy, and proteostasis imbalance in cancer.

Purpose of the Study:

  • To identify and analyze poorly investigated Hsp90 clients relevant to cancer processes.
  • To move beyond commonly studied Hsp90 targets in cancer research.
  • To propose novel therapeutic targets and diagnostic markers by examining 'unusual suspects'.

Main Methods:

  • Development of a workflow to select understudied Hsp90 client proteins in cancer.
  • Review and analysis of selected proteins based on their relation to cancer processes.
  • Literature review focusing on Hsp90 client proteins beyond established cancer drivers.

Main Results:

  • Identification of numerous Hsp90 client proteins implicated in cancer.
  • Highlighting a gap in the investigation of many Hsp90 clients.
  • Demonstrating the potential of understudied proteins as therapeutic or diagnostic candidates.

Conclusions:

  • Hsp90 plays a critical role in maintaining proteostasis in cancer cells.
  • Many Hsp90 clients remain underexplored as potential cancer therapies.
  • Revisiting these 'unusual suspects' could yield novel strategies for cancer treatment and diagnosis.
Keywords:
Hsp90KinaseMolecular chaperoneOncogeneProtein–protein interactionRegulationTranscription factorTumor suppressor

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