Targeting HSP90 for cancer therapy

D. Mahalingam, R. Swords, J. S. Carew, S. T. Nawrocki, K. Bhalla, F. J. Giles

Research output: Contribution to journalShort surveypeer-review

248 Scopus citations


Heat-shock proteins (HSPs) are molecular chaperones that regulate protein folding to ensure correct conformation and translocation and to avoid protein aggregation. Heat-shock proteins are increased in many solid tumours and haematological malignancies. Many oncogenic proteins responsible for the transformation of cells to cancerous forms are client proteins of HSP90. Targeting HSP90 with chemical inhibitors would degrade these oncogenic proteins, and thus serve as useful anticancer agents. This review provides an overview of the HSP chaperone machinery and the structure and function of HSP90. We also highlight the key oncogenic proteins that are regulated by HSP90 and describe how inhibition of HSP90 could alter the activity of multiple signalling proteins, receptors and transcriptional factors implicated in carcinogenesis.

Original languageEnglish (US)
Pages (from-to)1523-1529
Number of pages7
JournalBritish journal of cancer
Issue number10
StatePublished - May 19 2009
Externally publishedYes


  • AKT
  • EGFR
  • HER-2
  • Heat-shock proteins
  • Tumour suppressor genes
  • VEGF

ASJC Scopus subject areas

  • Oncology
  • Cancer Research


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