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Characterization of Microtubule-Associated Proteins (MAPs) and Tubulin Interactions by Isothermal Titration Calorimetry (ITC)

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Microcalorimetry of Biological Molecules

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1964))

Abstract

Microtubules are highly dynamic structures which play a central role in many cellular processes such as cell division, intracellular transport, and migration. Their dynamics is tightly regulated by stabilizing and destabilizing microtubule-associated proteins (MAPs), such as tau and stathmin. Many approaches have been developed to study interactions between tubulin and MAPs. However, isothermal titration calorimetry (ITC) is the only direct thermodynamic method that enables a full thermodynamic characterization of the interaction after a single titration experiment. We provide here the protocols to apply ITC to tubulin interaction with either stathmin or tau, which will help to avoid the common pitfalls in this very powerful and sensitive method.

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Correspondence to François Devred .

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Tsvetkov, P.O., La Rocca, R., Malesinski, S., Devred, F. (2019). Characterization of Microtubule-Associated Proteins (MAPs) and Tubulin Interactions by Isothermal Titration Calorimetry (ITC). In: Ennifar, E. (eds) Microcalorimetry of Biological Molecules. Methods in Molecular Biology, vol 1964. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-9179-2_12

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  • DOI: https://doi.org/10.1007/978-1-4939-9179-2_12

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-9178-5

  • Online ISBN: 978-1-4939-9179-2

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