Quantification of Membrane Protein Dynamics and Interactions in Plant Cells by Fluorescence Correlation Spectroscopy

Deciphering the dynamics of protein and lipid molecules on appropriate spatial and temporal scales may shed light on protein function and membrane organization. However, traditional bulk approaches cannot unambiguously quantify the extremely diverse mobility and interactions of proteins in living cells. Fluorescence correlation spectroscopy (FCS) is a powerful technique to describe events that occur at the single-molecule level and on the nanosecond to second timescales; therefore, FCS can provide data on the heterogeneous organization of membrane systems. FCS can also be combined with other microscopy techniques, such as super-resolution techniques. More importantly, FCS is minimally invasive, which makes it an ideal approach to detect the heterogeneous distribution and dynamics of key proteins during development. In this review, we give a brief introduction about the development of FCS and summarize the significant contributions of FCS in understanding the organization of plant cell membranes and the dynamics and interactions of membrane proteins. We also discuss the potential applications of this technique in plant biology.