Lipid miscibility phase separation has long been considered to be a central element of cell membrane organization. More recently, protein condensation phase transitions, into three-dimensional droplets or in two-dimensional lattices on membrane surfaces, have emerged as another important organizational principle within cells. Here, we reconstitute the linker for activation of T cells (LAT):growth-factor-receptor-bound protein 2 (Grb2):son of sevenless (SOS) protein condensation on the surface of giant unilamellar vesicles capable of undergoing lipid phase separations. Our results indicate that the assembly of the protein condensate on the membrane surface can drive lipid phase separation. This phase transition occurs isothermally and is governed by tyrosine phosphorylation on LAT. Furthermore, we observe that the induced lipid phase separation drives localization of the SOS substrate, K-Ras, into the LAT:Grb2:SOS protein condensate.

中文翻译：

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耦合膜脂混溶性和磷酸酪氨酸驱动的蛋白质凝聚相变

脂质混溶性相分离长期以来一直被认为是细胞膜组织的核心要素。最近，蛋白质凝聚相变，变成三维液滴或膜表面上的二维晶格，已成为细胞内另一个重要的组织原理。在这里，我们重建了用于激活 T 细胞 (LAT) 的链接器：生长因子受体结合蛋白 2 (Grb2)：在能够进行脂质相分离的巨型单层囊泡表面上的七少 (SOS) 蛋白凝聚的儿子。我们的结果表明，蛋白质凝聚物在膜表面的组装可以驱动脂质相分离。这种相变是等温发生的，并受 LAT 上的酪氨酸磷酸化控制。此外，