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Strategies for stalling malignancy: targeting cancer's addiction to Hsp90

Chrisostomos Prodromou1

  • 1Section of Structural Biology, The Institute of Cancer Research, Chester Beatty Laboratories, London SW3 6JB, UK. chris.prodromou@icr.ac.uk

Current Topics in Medicinal Chemistry
|October 29, 2009
PubMed

Insights

Heat shock protein 90 (Hsp90) aids cancer cell survival by stabilizing mutated proteins. Targeting Hsp90 offers a promising anticancer strategy by disrupting this essential chaperone machinery.

Area of Science:

  • Molecular Biology
  • Oncology
  • Drug Discovery

Background:

  • Heat shock protein 90 (Hsp90) is crucial for the maturation and activation of client proteins.
  • Mutated or deregulated signaling proteins, often dependent on Hsp90, can drive oncogenesis.
  • Hsp90's essential role in maintaining malignancy makes it a significant anticancer target.

Purpose of the Study:

  • To review potential drug targets within the Hsp90 chaperone machine.
  • To leverage structural knowledge of Hsp90 for drug development.
  • To identify strategies for disrupting Hsp90 function to promote anti-cancer activity.

Main Methods:

  • Review of current structural data of the Hsp90 chaperone machine.
  • Analysis of Hsp90's role in stabilizing oncogenic client proteins.
  • Identification of potential inhibition points in Hsp90's functional cycle.

Main Results:

  • Hsp90 client proteins are frequently mutated or deregulated in cancer.
  • Cancer cells exhibit a strong dependence on Hsp90 for survival and proliferation.
  • Disruption of Hsp90 function has demonstrated efficacy in killing cancer cells.

Conclusions:

  • Hsp90 is a critical 'axle in a wheel' for oncogenic pathways.
  • Targeting Hsp90 represents a viable therapeutic strategy for various cancers.
  • Further exploration of Hsp90 structural biology can guide the development of novel anticancer drugs.

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