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Cell membranes are laterally organized into functionally discrete domains that include the cholesterol-dependent membrane "rafts," and which function in regulating the association of membrane proteins with other factors and their activity.For example,our earlier studies showed the Src kinase Lck is selectively inhibited during association with raft domains,and this is due at least in part to sequestering from the membrane phosphatase CD45.However,the mechanisms regulating protein associations with membrane rafts and other types of domains remain unresolved and controversial.Accordingly,we used fluorescence resonance energy transfer (FRET) to provide nanometer resolution of co-association of fluorescent membrane markers within raft and nonrafl fractions of the outer membrane.