The study investigates the structure of raft domains in the plasma membrane of non-polarized cells, focusing on the lateral assemblies of glycolipids and cholesterol, known as "rafts." The researchers used cross-linking techniques to study the patching behavior of raft markers (defined by their insolubility in Triton X-100) and non-raft markers. They found that patches of raft markers, such as GPI-anchored placental alkaline phosphatase (PLAP) and influenza virus hemagglutinin (HA), overlapped extensively in BHK and Jurkat T-lymphoma cells. In contrast, patches of raft components and non-raft markers like transferrin receptor were sharply separated. The study also revealed that cholesterol depletion abrogated the segregation of raft and non-raft patches, suggesting that the immiscibility of different lipid phases causes their separation. Additionally, patches of GPI-anchored PLAP accumulated src-like protein tyrosine kinase fyn, which is thought to be anchored in the cytoplasmic leaflet of raft domains. These findings support the view that raft domains in non-polarized cells are normally small and highly dispersed, but their size can be modulated by oligomerization of raft components. The results provide evidence for specific lipid-lipid and lipid-protein interactions governing raft dispersion and clustering.The study investigates the structure of raft domains in the plasma membrane of non-polarized cells, focusing on the lateral assemblies of glycolipids and cholesterol, known as "rafts." The researchers used cross-linking techniques to study the patching behavior of raft markers (defined by their insolubility in Triton X-100) and non-raft markers. They found that patches of raft markers, such as GPI-anchored placental alkaline phosphatase (PLAP) and influenza virus hemagglutinin (HA), overlapped extensively in BHK and Jurkat T-lymphoma cells. In contrast, patches of raft components and non-raft markers like transferrin receptor were sharply separated. The study also revealed that cholesterol depletion abrogated the segregation of raft and non-raft patches, suggesting that the immiscibility of different lipid phases causes their separation. Additionally, patches of GPI-anchored PLAP accumulated src-like protein tyrosine kinase fyn, which is thought to be anchored in the cytoplasmic leaflet of raft domains. These findings support the view that raft domains in non-polarized cells are normally small and highly dispersed, but their size can be modulated by oligomerization of raft components. The results provide evidence for specific lipid-lipid and lipid-protein interactions governing raft dispersion and clustering.