Cosson P, Letourneur F
Basel Institute for Immunology, Switzerland.
Science. 1994 Mar 18;263(5153):1629-31. doi: 10.1126/science.8128252.
Although signals for retention in the endoplasmic reticulum (ER) have been identified in the cytoplasmic domain of various ER-resident type I transmembrane proteins, the mechanisms responsible for ER retention are still unknown. Yeast and mammalian ER retention motifs interacted specifically in cell lysates with the coatomer, a polypeptide complex implicated in membrane traffic. Mutations that affect the ER retention capacity of the motifs also abolished binding of the coatomer. These results suggest a role for the coatomer in the retrieval of transmembrane proteins to the ER in both yeast and mammals.
尽管在内质网（ER）驻留的多种I型跨膜蛋白的胞质结构域中已鉴定出内质网保留信号，但内质网保留的机制仍不清楚。酵母和哺乳动物的内质网保留基序在细胞裂解物中与外套膜蛋白特异性相互作用，外套膜蛋白是一种参与膜运输的多肽复合物。影响这些基序内质网保留能力的突变也消除了外套膜蛋白的结合。这些结果表明，外套膜蛋白在酵母和哺乳动物中跨膜蛋白向内质网的回收过程中发挥作用。
