Related Experiment Video
Updated: May 30, 2026

Dual-Color Fluorescence Cross-Correlation Spectroscopy to Study Protein-Protein Interaction and Protein Dynamics in Live Cells
Published on: December 11, 2021
Fluorescence fluctuation analysis of receptor kinase dimerization
Mark A Hink1, Sacco C de Vries, Antonie J W G Visser
1Department of Molecular Cytology, van Leeuwenhoek Centre for Advanced Microscopy (LCAM), University of Amsterdam, Amsterdam, The Netherlands. m.a.hink@uva.nl
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.
More Related Videos
14:09Fluorescence Biomembrane Force Probe: Concurrent Quantitation of Receptor-ligand Kinetics and Binding-induced Intracellular Signaling on a Single Cell
Published on: August 4, 2015
10:43Oligomerization Dynamics of Cell Surface Receptors in Living Cells by Total Internal Reflection Fluorescence Microscopy Combined with Number and Brightness Analysis
Published on: November 6, 2019