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Molecular Chaperones pp 67–74Cite as

Detecting HSP90 Phosphorylation

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 787))

Abstract

Heat-shock protein 90 (HSP90) is an essential molecular chaperone in eukaryotes. It is important for chaperoning proteins that are important determinants of multistep carcinogenesis. HSP90’s ATPase activity is associated with its chaperone function. Co-chaperones as well as posttranslational modifications (phosphorylation, acetylation, and S-nitrosylation) are important for regulating its ATPase activity. Yeast can be used to express and purify HSP90 and also detect its phosphorylation by pan-phosphoserine or phosphothreonine antibodies.

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Author information

Authors and Affiliations

  1. Urologic Oncology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA

    Mehdi Mollapour & Len Neckers

Authors
  1. Mehdi Mollapour
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  2. Len Neckers
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Corresponding author

Correspondence to Len Neckers .

Editor information

Editors and Affiliations

  1. Beth Israel Deaconess Medical Center, Department of Radiation Oncology, Harvard Medical School, Brookline Ave 330, Boston, 02215, Massachusetts, USA

    Stuart K. Calderwood

  2. National Cancer Institute, Urologic Oncology Branch, National Institutes of Health, Rockville Pike 9000, Bethesda, 20814, Maryland, USA

    Thomas L. Prince

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Mollapour, M., Neckers, L. (2011). Detecting HSP90 Phosphorylation. In: Calderwood, S., Prince, T. (eds) Molecular Chaperones. Methods in Molecular Biology, vol 787. Humana Press. https://doi.org/10.1007/978-1-61779-295-3_5

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  • DOI: https://doi.org/10.1007/978-1-61779-295-3_5

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  • Publisher Name: Humana Press

  • Print ISBN: 978-1-61779-294-6

  • Online ISBN: 978-1-61779-295-3

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