Cell surface receptors distinguish specific stimuli from biological noise, and underlying mechanisms depend on the organization of plasma membrane components. We exploited the statistical robustness of multiplexed Imaging Fluorescence Correlation Spectroscopy (ImFCS), to evaluate subtle diffusion differences of key components in the early stage of mast cell signaling by measuring their diffusion in live cells: FcεRI receptor for immunoglobulin E (IgE), tyrosine kinase Lyn anchored to the membrane inner leaflet, and transmembrane phosphatase PTPα. Our results confirm that the nanoscale distribution of signaling proteins is coordinately rearranged after the receptor is stimulated, such that changes in relatively weak interactions serve to transmit the signal across the membrane.
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