Single-molecule tracking study of the mechanisms of signal transduction in lipid rafts of cell plasma membranes

结果表明，在稳态细胞膜中，gpi锚定蛋白基于胞外蛋白-蛋白相互作用形成瞬时同型二聚体。在存在蛋白质-蛋白质相互作用的情况下，脂质相互作用被发现促进了同型二聚体的形成，而在没有蛋白质相互作用的情况下没有观察到这一点。此外，我们还发现gpi锚定受体结扎后形成了非常稳定的同质低聚物，这些低聚物招募了其他筏脂、神经节苷脂，并在低聚物中诱导了筏状结构。低聚物中筏状结构的形成对于细胞内钙反应等下游信号传导至关重要。

It has turned out that in steady-state cell plasma membranes, GPI-anchored proteins formed transient homo-dimers based on the extracellular protein-protein interactions. In the presence of protein-protein interactions, lipid interactions were found to facilitate the formation of the homo-dimers, while this was not observed in the absence of the protein interactions. Furthermore, it was found that upon ligation of GPI-anchored receptors, very stable homo-oligomers were formed, the oligomers recruited other raft lipid, ganglioside, and induced raft-like structure in the oligomers. The formation of the raft-like structure in the oligomers was essential for the downstream signaling such as intracellular calcium response.