Abstract
Dynamic instability is a hallmark of the microtubule cytoskeleton. In order to regulate microtubule dynamics in vivo, a varied host of microtubule-associated proteins are mobilized to promote microtubule nucleation, growth, stabilization, catastrophe, depolymerization, rescue, and severing. To confer these various functions, cytoskeletal regulators have highly tuned affinities for tubulin, recognizing the unpolymerized αβ-tubulin heterodimer, dynamic microtubule lattice, stabilized microtubule lattice, or a combination therein. The protocols presented here probe αβ-tubulin and microtubule binding using gel filtration and cosedimentation, respectively.
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Acknowledgments
The authors would like to thank Dr. Stephen Rogers for advice. This work was supported by a Basil O’Connor Research Starter Grant from the March of Dimes.
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Campbell, J.N., Slep, K.C. (2011). αβ-Tubulin and Microtubule-Binding Assays. In: Straube, A. (eds) Microtubule Dynamics. Methods in Molecular Biology, vol 777. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-252-6_6
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DOI: https://doi.org/10.1007/978-1-61779-252-6_6
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