Kreis T E, Pepperkok R
Department of Cell Biology, University of Geneva, Switzerland.
Curr Opin Cell Biol. 1994 Aug;6(4):533-7. doi: 10.1016/0955-0674(94)90073-6.
Transport of newly synthesized material from the endoplasmic reticulum (ER) towards the Golgi complex, through the Golgi cisternae, and out of the trans-Golgi network (TGN) is thought to be mediated by vesicular carriers. Different types of vesicle are involved in this biosynthetic membrane traffic. All are coated with protein complexes on their cytoplasmic surface. COP-coated vesicles have recently been implicated in transport of cargo from the ER to the TGN, and clathrin-coated vesicles from the TGN to endosomes, but the carriers moving material to the cell surface are still unknown. Sequence homologies between subunits of the COP- and the clathrin-adaptor complexes suggest that coat proteins may belong to a family of proteins with related functions. The precise role of the coat proteins is not fully understood, although they have been implicated in clustering of cargo into buds and in budding of vesicles. In addition, coat proteins may play an essential role in targeting of transport intermediates and may serve to regulate membrane fusion.
新合成的物质从内质网（ER）向高尔基体复合体运输，穿过高尔基池，并从反式高尔基体网络（TGN）输出，这一过程被认为是由囊泡载体介导的。不同类型的囊泡参与了这种生物合成膜运输。所有囊泡在其细胞质表面都覆盖有蛋白质复合体。COP包被囊泡最近被认为参与了货物从内质网到反式高尔基体网络的运输，而网格蛋白包被囊泡则参与了从反式高尔基体网络到内体的运输，但将物质运输到细胞表面的载体仍不清楚。COP和网格蛋白衔接复合体亚基之间的序列同源性表明，包被蛋白可能属于具有相关功能的蛋白质家族。尽管包被蛋白已被认为与货物聚集到芽中以及囊泡出芽有关，但其确切作用尚未完全了解。此外，包被蛋白可能在运输中间体的靶向中起重要作用，并可能用于调节膜融合。
