Krueger J G, Wang E, Garber E A, Goldberg A R
Proc Natl Acad Sci U S A. 1980 Jul;77(7):4142-6. doi: 10.1073/pnas.77.7.4142.
We have investigated the intracellular location of pp60src in Rous sarcoma virus-transformed rat cells (RR1022) by indirect immunofluorescence microscopy and cell fractionation. Immunofluorescence data suggest that pp60src is predominantly associated with the nuclear envelope and the juxtanuclear reticular membrane structures. The bulk of pp60src and of the associated phosphotransferase activity fractionated with nuclei and not with plasma membranes in disrupted cells. This localization contrasts strikingly with the association of pp60src with the plasma membrane of Rous sarcoma virus-transformed chicken fibroblasts. We propose that pp60src is a membrane protein that associates with cellular membranes through hydrophobic regions and that this membrane association is a general feature of the interaction of pp60src with avian and mammalian cells. Although there are major differences in the intracellular localizations of pp60src, it may interact with cellular membranes through one or more NH2-terminal hydrophobic regions.
我们通过间接免疫荧光显微镜和细胞分级分离法研究了劳氏肉瘤病毒转化的大鼠细胞（RR1022）中pp60src的细胞内定位。免疫荧光数据表明，pp60src主要与核膜和近核网状膜结构相关。在破碎的细胞中，大部分pp60src及其相关的磷酸转移酶活性与细胞核一起分级分离，而不是与质膜一起。这种定位与pp60src与劳氏肉瘤病毒转化的鸡成纤维细胞质膜的关联形成了鲜明对比。我们提出，pp60src是一种通过疏水区域与细胞膜结合的膜蛋白，并且这种膜结合是pp60src与禽类和哺乳动物细胞相互作用的一个普遍特征。尽管pp60src的细胞内定位存在主要差异，但它可能通过一个或多个NH2末端疏水区域与细胞膜相互作用。
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