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Characterization of STAT Self-Association by Analytical Ultracentrifugation

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JAK-STAT Signalling

Part of the book series: Methods in Molecular Biology ((MIMB,volume 967))

Abstract

Multiple experimental tools have demonstrated that cytokine-induced STAT activation entails the transition of dimer conformations rather than de novo dimerization. In this chapter, we describe the utilization of analytical ultracentrifugation (AUC) as a powerful technique for the quantitative analysis of hydro- and thermodynamic properties of STAT proteins in solution. These studies provided a quantitative understanding of dimer stability and conformational transitions associated with the activation of STAT1.

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Acknowledgment

We thank Borries Demeler (University of Texas Health Science Center at San Antonio) for critical reading and comments. This work was supported by BBSRC grant BB/GO019290/1.

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Authors and Affiliations

  1. School of Biomedical Sciences, University of Nottingham Medical School, Nottingham, UK

    Nikola Wenta & Uwe Vinkemeier

Authors
  1. Nikola Wenta
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  2. Uwe Vinkemeier
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Editors and Affiliations

  1. Walter and Eliza Hall Institute, Royal Parade 1G, Parkville, 3050, Victoria, Australia

    Sandra E. Nicholson

  2. Walter and Eliza Hall Institute, Royal Parade 1G, Parkville, 3050, Victoria, Australia

    Nicos A. Nicola

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Wenta, N., Vinkemeier, U. (2013). Characterization of STAT Self-Association by Analytical Ultracentrifugation. In: Nicholson, S., Nicola, N. (eds) JAK-STAT Signalling. Methods in Molecular Biology, vol 967. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-242-1_15

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  • DOI: https://doi.org/10.1007/978-1-62703-242-1_15

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-62703-241-4

  • Online ISBN: 978-1-62703-242-1

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