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Significance Lipid organization of the plasma membrane is known to be important for facilitating protein interactions in transmembrane signaling. However, the orchestration of these interactions in live cells remains elusive. We employed imaging fluorescence correlation spectroscopy (ImFCS) to systemically investigate the interplay of lipids and proteins during mast cell signaling, initiated as phosphorylation of antigen-crosslinked immunoglobulin E–receptor (IgE-FcεRI) complexes by lipid-anchored Lyn kinase. We found that stabilized liquid ordered-like nanodomains around clustered FcεRI—which can be accessed by Lyn kinase but not by transmembrane phosphatase—provide essential spatial filtering that augments Lyn’s binding and phosphorylating FcεRI while suppressing dephosphorylation by phosphatase. ImFCS provides quantitative evidence of the functional link between lipid-based membrane organization and transmembrane signaling in live cells.

Lipid-based and protein-based interactions synergize transmembrane signaling stimulated by antigen clustering of IgE receptors