Whitney J A, Gomez M, Sheff D, Kreis T E, Mellman I
Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520-8002, USA.
Cell. 1995 Dec 1;83(5):703-13. doi: 10.1016/0092-8674(95)90183-3.
Endosomes are intermediates for a complex series of sorting and transport events that occur during receptor-mediated endocytosis. These involve the recognition of targeting determinants on the cytoplasmic domains of many membrane proteins as well as the formations of specific transport vesicles. Accordingly, endosome function is likely to be governed by the regulated assembly of cytoplasmic coat complexes. We have found that, in vitro, endosomes recruit a characteristic set of cytoplasmic proteins in a GTP gamma S-stimulated and brefeldin A-sensitive fashion. Among these are members of the COP-I and ARF families of coat proteins. In addition, endosomes were also found to assemble distinct, clathrin-like coats. Since microinjection of antibodies to beta-COP inhibits the entry of enveloped viruses via the endocytic pathway, it is apparent that the recruitment of COP-I or COP-I-related proteins plays an important role in the function of endosomes in intact cells.
内体是受体介导的内吞作用过程中一系列复杂分选和运输事件的中间体。这些事件涉及对许多膜蛋白细胞质结构域上靶向决定簇的识别以及特定运输小泡的形成。因此,内体功能可能受细胞质包被复合物的有序组装调控。我们发现,在体外,内体以GTPγS刺激且布雷菲德菌素A敏感的方式募集一组特定的细胞质蛋白。其中包括COP-I和ARF包被蛋白家族的成员。此外,还发现内体组装不同的、网格蛋白样包被。由于显微注射抗β-COP抗体可抑制包膜病毒通过内吞途径进入,显然COP-I或COP-I相关蛋白的募集在完整细胞内体功能中起重要作用。