  Central to understanding membrane bound cell signaling is to quantify how the
membrane ultra-structure consisting of transient spatial domains modulates
signaling and how the signaling influences this ultra-structure. Yet, measuring
the association of membrane proteins with domains in living, intact cells poses
considerable challenges. Here, we describe a non-destructive method to quantify
protein-lipid domain and protein cytoskeleton interactions in single, intact
cells enabling continuous monitoring of the protein domains interaction over
time during signaling.
