Kozma L M, Reynolds A B, Weber M J
Department of Microbiology and Cancer Center, University of Virginia School of Medicine, Charlottesville 22908.
Mol Cell Biol. 1990 Feb;10(2):837-41. doi: 10.1128/mcb.10.2.837-841.1990.
The level of tyrosine phosphorylation of cellular glycoproteins isolated by wheat germ agglutinin chromatography in cells infected with a variety of kinase-positive/transformation-defective src mutants was examined in an effort to identify cellular membrane proteins whose phosphorylation correlates with phenotypic transformation. We have identified two glycoproteins, with molecular masses of 95 and 135 kilodaltons, whose phosphorylation correlates with morphological transformation, growth in soft agar, and an increase in the rate of 2-deoxyglucose uptake. The strong correlation obtained between transformation and phosphorylation of these proteins suggests that they may be substrates for pp60src which are important in the process of transformation.
为了鉴定其磷酸化与表型转化相关的细胞膜蛋白，我们检测了用麦胚凝集素层析法从感染多种激酶阳性/转化缺陷型src突变体的细胞中分离出的细胞糖蛋白的酪氨酸磷酸化水平。我们鉴定出两种糖蛋白，分子量分别为95和135千道尔顿，它们的磷酸化与形态转化、软琼脂中的生长以及2-脱氧葡萄糖摄取速率的增加相关。这些蛋白的转化与磷酸化之间的强相关性表明，它们可能是pp60src的底物，在转化过程中起重要作用。
