Abstract
Receptor kinases are essential for the cellular perception of signals. The classical model for activation of the receptor kinase involves dimerization, induced by the binding of the ligand. The mechanisms by which plant receptors transduce signals across the cell surface are largely unknown but plant receptors seem to dimerize as well. In this chapter, we describe two fluorescence fluctuation techniques, fluorescence cross-correlation spectroscopy and photon counting histogram analysis, to study the oligomerization state of receptor kinases in living plant cells in a quantitative manner.
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Acknowledgments
The authors would like to thank Khalid Shah, Eugenia Russinova, Frank van Breukelen, and Jeroen Pouwels for assistance during the experiments and Jan Willem Borst for valuable discussions. This work was supported by the Council of Earth and Life Sciences of the Netherlands Organization for Scientific Research (ALW-NWO).
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Hink, M.A., de Vries, S.C., Visser, A.J.W.G. (2011). Fluorescence Fluctuation Analysis of Receptor Kinase Dimerization. In: Dissmeyer, N., Schnittger, A. (eds) Plant Kinases. Methods in Molecular Biology, vol 779. Humana, Totowa, NJ. https://doi.org/10.1007/978-1-61779-264-9_11
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DOI: https://doi.org/10.1007/978-1-61779-264-9_11
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