Tyrosine phosphorylation within the amino-terminal domain of pp60c-src molecules associated with polyoma virus middle-sized tumor antigen.
Tyrosine phosphorylation within the amino-terminal domain of pp60c-src molecules associated with polyoma virus middle-sized tumor antigen.
复制标题
与多瘤病毒中型肿瘤抗原相关的 pp60c-src 分子氨基末端结构域内的酪氨酸磷酸化。
DOI：
10.1073/pnas.82.14.4568
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发表时间：
1985
影响因子：
11.1
通讯作者：
Israel,MA
中科院分区：
文献类型：
--
作者：
Yonemoto,W;Jarvis-Morar,M;Brugge,JS;Bolen,JB;Israel,MA
我们已经研究了在多瘤病毒转化细胞中与多瘤病毒中等大小肿瘤抗原相关的细胞src蛋白（pp 60 c-src）分子的体外磷酸化。这些pp 60 c-src分子具有增强的酪氨酰激酶活性，迁移aberrantly NaDodSO 4/聚丙烯酰胺凝胶上，并包含一个新的位点的酪氨酸磷酸化的氨基末端区域内的分子。与中等大小肿瘤抗原无关的pp 60 c-src分子仅在pp 60 c-src羧基末端结构域内的酪氨酸残基上磷酸化。一个类似的修改形式的中等大小的肿瘤抗原相关的pp 60 c-src蛋白质中检测多瘤病毒转化的细胞裂解物在体内标记的[32 P]正磷酸盐在原钒酸钠的存在下，磷酸酪氨酸磷酸酶的抑制剂。
We have examined the in vitro phosphorylation of cellular src protein (pp60c-src) molecules associated with the polyoma virus middle-sized tumor antigen in polyoma virus-transformed cells. These pp60c-src molecules possessed an enhanced tyrosyl kinase activity, migrated aberrantly on NaDodSO4/polyacrylamide gels, and contained a novel site of tyrosine phosphorylation within the amino-terminal region of the molecule. The pp60c-src molecules not associated with the middle-sized tumor antigen were phosphorylated exclusively on a tyrosine residue within the carboxyl-terminal domain of pp60c-src. A similar modified form of the middle-sized tumor antigen-associated pp60c-src protein was detected in lysates from polyoma virus-transformed cells labeled in vivo with [32P]orthophosphate in the presence of sodium orthovanadate, an inhibitor of phosphotyrosyl phosphatases.