Pepperkok R, Scheel J, Horstmann H, Hauri H P, Griffiths G, Kreis T E
European Molecular Biology Laboratory, Heidelberg, Federal Republic of Germany.
Cell. 1993 Jul 16;74(1):71-82. doi: 10.1016/0092-8674(93)90295-2.
Microinjection of antibodies against a synthetic peptide of a non-clathrin-coated vesicle-associated coat protein, beta-COP, blocks transport of a temperature-sensitive vesicular stomatitis virus glycoprotein (ts-O45-G) to the cell surface. Transport is inhibited upon release of the viral glycoprotein from temperature blocks at 39.5 degrees C (endoplasmic reticulum [ER]) and 15 degrees C (intermediate compartment), but not at 20 degrees C (trans-Golgi network). Ts-O45-G is arrested in tubular membrane structures containing p53 at the interface of the ER and the Golgi stack. This is consistent with inhibition of acquisition of endoglycosidase H resistance of ts-O45-G in injected cells. Secretion of endogenous proteins and maturation of cathepsin D are also inhibited. These data provide in vivo evidence that beta-COP has an important function in biosynthetic membrane traffic in mammalian cells.
显微注射针对非网格蛋白包被囊泡相关包被蛋白β-COP的合成肽的抗体，可阻断温度敏感型水泡性口炎病毒糖蛋白（ts-O45-G）向细胞表面的转运。当病毒糖蛋白在39.5℃（内质网[ER]）和15℃（中间区室）从温度阻滞中释放时，转运受到抑制，但在20℃（反式高尔基体网络）时不受抑制。Ts-O45-G停滞在内质网和高尔基体堆叠界面处含有p53的管状膜结构中。这与注射细胞中ts-O45-G的内切糖苷酶H抗性获得受到抑制一致。内源性蛋白质的分泌和组织蛋白酶D的成熟也受到抑制。这些数据提供了体内证据，表明β-COP在哺乳动物细胞的生物合成膜运输中具有重要功能。
