Brown D A, Rose J K
Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06510.
Cell. 1992 Feb 7;68(3):533-44. doi: 10.1016/0092-8674(92)90189-j.
We show that a protein with a glycosylphosphatidyl inositol (GPI) anchor can be recovered from lysates of epithelial cells in a low density, detergent-insoluble form. Under these conditions, the protein is associated with detergent-resistant sheets and vesicles that contain other GPI-anchored proteins and are enriched in glycosphingolipids, but do not contain a basolateral marker protein. The protein is recovered in this complex only after it has been transported to the Golgi complex, suggesting that protein-sphingolipid microdomains form in the Golgi apparatus and plasma membrane and supporting the model proposed by Simons and colleagues for sorting of certain membrane proteins to the apical surface after intracellular association with glycosphingolipids.
我们发现，一种带有糖基磷脂酰肌醇（GPI）锚定的蛋白质能够以低密度、去污剂不溶性的形式从上皮细胞裂解物中回收。在这些条件下，该蛋白质与去污剂抗性片层和囊泡相关联，这些片层和囊泡含有其他GPI锚定蛋白且富含糖鞘脂，但不含有基底外侧标记蛋白。该蛋白质只有在被转运至高尔基体复合体后才会在这种复合物中被回收，这表明蛋白质 - 鞘脂微结构域在高尔基体和质膜中形成，并支持了西蒙斯及其同事提出的模型，即某些膜蛋白在细胞内与糖鞘脂结合后被分选至顶端表面。
