Barlowe C
Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03750, USA.
FEBS Lett. 1995 Aug 1;369(1):93-6. doi: 10.1016/0014-5793(95)00618-j.
Vesicle budding from the endoplasmic reticulum (ER) has been reconstituted with washed membranes and three soluble proteins: Sec13 complex, Sec23 complex and the small GTPase Sar1p. The proteins that drive this cell-free vesicle budding reaction form an approximately 10 nm thick electron dense coat on ER-derived vesicles. Although the overall mechanism of membrane budding driven by various cytoplasmic coats appears similar, the constituents of this new membrane coat are molecularly distinct from the non-clathrin coat (COP) involved in intra-Golgi transport and the clathrin-containing coats. The new vesicle coat has been termed COPII.
内质网(ER)的囊泡出芽过程已通过洗涤后的膜以及三种可溶性蛋白质进行了重构:Sec13复合体、Sec23复合体和小GTP酶Sar1p。驱动这种无细胞囊泡出芽反应的蛋白质在内质网衍生的囊泡上形成了一层约10纳米厚的电子致密衣被。尽管由各种细胞质衣被驱动的膜出芽的总体机制似乎相似,但这种新的膜衣被的组成成分在分子层面上与参与高尔基体内运输的非网格蛋白衣被(COP)以及含网格蛋白的衣被不同。这种新的囊泡衣被被称为COPII。