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Structure–Functions of HspB1 (Hsp27)

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Molecular Chaperones

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

Abstract

Human HspB1 (also denoted Hsp27) is a well-known member, together with alphaB-crystallin, of the small heat-shock (or stress) proteins (sHsps) (20–40 kDa). In this chapter, I describe procedures for testing the oligomeric and phosphorylation patterns of HspB1 as well as its interaction with specific partner/client polypeptides using tissue culture cells genetically modified to express different levels of this protein. The procedures have been developed in my laboratory and could be used in any well-established cellular laboratory. In addition, the different procedures presented here could be extended to test the nine other human sHsp members as well as sHsps from other species.

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Author information

Authors and Affiliations

  1. Stress, Chaperons, and Cell Death Laboratory, CNRS UMR 5534, Claude Bernard University Lyon 1, Villeurbanne, France

    André-Patrick Arrigo

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  1. André-Patrick Arrigo
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Correspondence to André-Patrick Arrigo .

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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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Arrigo, AP. (2011). Structure–Functions of HspB1 (Hsp27). 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_9

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  • DOI: https://doi.org/10.1007/978-1-61779-295-3_9

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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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