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首页> 外文期刊>Molecular and Cellular Biology >Cell surface expression of v-fms-coded glycoproteins is required for transformation.
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Cell surface expression of v-fms-coded glycoproteins is required for transformation.

机译：v-fms编码的糖蛋白的细胞表面表达是转化所必需的。

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摘要

The viral oncogene v-fms encodes a transforming glycoprotein with in vitro tyrosine-specific protein kinase activity. Although most v-fms-coded molecules remain internally sequestered in transformed cells, a minor population of molecules is transported to the cell surface. An engineered deletion mutant lacking 348 base pairs of the 3.0-kilobase-pair v-fms gene encoded a polypeptide that was 15 kilodaltons smaller than the wild-type v-fms gene product. The in-frame deletion of 116 amino acids was adjacent to the transmembrane anchor peptide located near the middle of the predicted protein sequence and 432 amino acids from the carboxyl terminus. The mutant polypeptide acquired N-linked oligosaccharide chains, was proteolytically processed in a manner similar to the wild-type glycoprotein, and exhibited an associated tyrosine-specific protein kinase activity in vitro. However, the N-linked oligosaccharides of the mutant glycoprotein were not processed to complex carbohydrate chains, and the glycoprotein was not detected at the cell surface. Cells expressing high levels of the mutant glycoprotein did not undergo morphological transformation and did not form colonies in semisolid medium. The transforming activity of the v-fms gene product therefore appears to be mediated through target molecules on the plasma membrane.
机译：病毒癌基因v-fms编码具有体外酪氨酸特异性蛋白激酶活性的转化糖蛋白。尽管大多数v-fms编码的分子在内部保留在转化细胞中，但少数分子被转运到细胞表面。缺少348个碱基对的3.0-碱基对v-fms基因的工程缺失突变体编码的多肽比野生型v-fms基因产物小15道尔顿。框内116个氨基酸的缺失与位于预测蛋白序列中部附近的跨膜锚肽和来自羧基末端的432个氨基酸相邻。突变多肽获得的N-连接的寡糖链，以类似于野生型糖蛋白的方式进行蛋白水解加工，并在体外表现出相关的酪氨酸特异性蛋白激酶活性。但是，突变糖蛋白的N-连接寡糖未加工成复杂的碳水化合物链，并且在细胞表面未检测到糖蛋白。表达高水平突变糖蛋白的细胞未进行形态转化，也未在半固体培养基中形成菌落。因此，v-fms基因产物的转化活性似乎是通过质膜上的靶分子介导的。

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