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Escape from HER-family tyrosine kinase inhibitor therapy by the kinase-inactive HER3

Author

Listed:
  • Natalia V. Sergina

    (University of California)

  • Megan Rausch

    (University of California)

  • Donghui Wang

    (University of California)

  • Jimmy Blair

    (University of California)

  • Byron Hann

    (University of California)

  • Kevan M. Shokat

    (University of California)

  • Mark M. Moasser

    (University of California)

Abstract

Targeted cancer therapies Certain tyrosine kinases are overactive in many cancers, and drugs that inhibit them, such as the leukaemia treatment imatinib, can be successful. But they don't work for all tyrosine kinase-driven cancers, and new work points to a possible reason why. The kinase HER2 is frequently overactive in breast cancers and signals through another family member, HER3. Sergina et al. find that when HER2 is partially blocked by kinase inhibitors, a feedback mechanism causes an increase of active HER3 at the plasma membrane where it continues to signal cancer cell proliferation. So more effective inhibitors that block HER2 completely, and reduce HER3 activity too, may be more effective cancer therapies.

Suggested Citation

  • Natalia V. Sergina & Megan Rausch & Donghui Wang & Jimmy Blair & Byron Hann & Kevan M. Shokat & Mark M. Moasser, 2007. "Escape from HER-family tyrosine kinase inhibitor therapy by the kinase-inactive HER3," Nature, Nature, vol. 445(7126), pages 437-441, January.
    • Handle: RePEc:nat:nature:v:445:y:2007:i:7126:d:10.1038_nature05474
    DOI: 10.1038/nature05474
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    Cited by:

    1. Harish Shankaran & Yi Zhang & Yunbing Tan & Haluk Resat, 2013. "Model-Based Analysis of HER Activation in Cells Co-Expressing EGFR, HER2 and HER3," PLOS Computational Biology, Public Library of Science, vol. 9(8), pages 1-15, August.

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